FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides. FUNCTION: Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GLTP family.


FUNCTION: Probably involved in ribonucleotide reductase function. SIMILARITY: Belongs to the NrdI family.


FUNCTION: Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 2 subfamily.


FUNCTION: A core subunit of photosystem II (PSII). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Ycf12 family.


SIMILARITY: Belongs to the RSRC2 family.


FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of fumigermin that inhibits germination of spores of the inducing S.rapamycinicus, and thus helps the fungus to defend resources in the shared habitat against a bacterial competitor (PubMed:32083553). May be involved in the secretion of fumigermin (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.


FUNCTION: Involved in the digestion of the blood meal. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M14 family.


FUNCTION: (Microbial infection) May prevent cell death upon A.alternata f.sp. lycopersici (AAL) toxin treatment. FUNCTION: (Microbial infection) Facilitates the development of the powdery mildew fungus E.cruciferarum. FUNCTION: Regulates the brassinosteroid (BR) signaling pathway that mediates cell elongation and organ morphogenesis (PubMed:19202280). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family.


FUNCTION: Probable GTP-binding protein that may be involved in cell development. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.


FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family.


FUNCTION: Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus Host nucleus, host nucleolus. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cleavage furrow. Cell projection, microvillus Note=Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.


FUNCTION: Plays a role in the different steps of crossover formation during meiotic recombination (PubMed:24891606, PubMed:32640224, PubMed:32555348). Participates in the crossover differentiation step of crossover-specific recombination intermediates through its interaction with PRR19 (PubMed:32555348). In addition, stimulates crossover formation through the interactions with RFC3 and RFC4 and simultaneously regulates cell-cycle progression through interactions with CDC34 and subsequent ubiquitination of WEE1 (PubMed:32640224). May also participates in an active deselection process that destabilizes or removes excess pre-CO intermediates (PubMed:24891606). SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome Note=Shuttles between the nucleus and cytoplasm in a stage-specific manner of prophase I cells (PubMed:32640224). Co-localized at crossover sites with PRR19 (PubMed:32555348).


FUNCTION: Functions in inorganic phosphate uptake, a phosphate-binding protein, although probably not the main uptake protein under phosphate starvation (By similarity). Part of the ABC transporter complex PstSACB involved in phosphate import (Probable). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Secreted Note=Present on the cell surface. SIMILARITY: Belongs to the PstS family.


FUNCTION: Structural protein that is not essential for the viral replication either in tissue culture or in its natural host. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the coronavirus I protein family.


FUNCTION: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan (PubMed:15661003, PubMed:32350117). O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance (PubMed:15661003). FUNCTION: Responsible for O-acetylation at the C(6)-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O- diacetylmuramic acid of the peptidoglycan. O-acetylation of the peptidoglycan is the major determinant for lysozyme resistance. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acyltransferase 3 family.


FUNCTION: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to the membrane through a conserved C-terminal amphipathic helix. SIMILARITY: Belongs to the FtsA/MreB family.


FUNCTION: Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD (PubMed:23170229, PubMed:25910242). Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA (PubMed:25910242). SIMILARITY: Belongs to the PanZ/PanM family.


FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.


FUNCTION: AcpB and AcpA regulate cap gene expression and capsule synthesis. SIMILARITY: Belongs to the AtxA/AcpA family.


FUNCTION: Associates with the spindle pole body and maintains a functional interface between the nuclear membrane and the microtubule motor proteins. Involved in chromosome segregation during meiosis where it associates with the telomeres. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nucleus membrane; Single-pass membrane protein.


SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family.


FUNCTION: Snake venom phospholipase A2 (PLA2) that inhibits neuromuscular transmission by blocking acetylcholine release from the nerve termini. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.


FUNCTION: Core component of the 3M complex, a complex required to regulate microtubule dynamics and genome integrity. It is unclear how the 3M complex regulates microtubules, it could act by controlling the level of a microtubule stabilizer. Required for localization of CUL7 to the centrosome. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.


SIMILARITY: Belongs to the UPF0355 family.


FUNCTION: Oxidase; part of the gene cluster that mediates the biosynthesis of hancockiamides, an unusual new family of N- cinnamoylated piperazines (PubMed:33242032). The NRPS hkm10 and the NmrA-like reductase hkm9 are proposed to convert two molecules of L-Phe to the intermediary piperazine called xenocockiamide A (Probable). Xenocockiamide A is then converted to hancockiamide D via a series of hydroxylations and O-methylations (Probable). The tyrosinase hkm6 may catalyze an aromatic hydroxylation, then the 2-oxoglutarate-dependent Fe(II) dioxygenase hkm4 and the FAD-dependent phenol hydroxylase hkm7 may catalyze consecutive hydroxylations to install 2 more hydroxy groups, and the methyltransferase hkm8 probably catalyzes two methylations using 2 molecules of S-adenosyl-L-methionine (SAM) (Probable). The NRPS hkm11 activates and transfers trans-cinnamate supplied by the PAL hkm12 to hancockiamide D and produces hancockiamide A (PubMed:33242032). NRPS Hkm11 has the flexibility to tolerate the bulky hancockiamide G as a substrate and the absence of the acetyl- transferase hkm3 opens up the opportunity for hkm11 to introduce a second N-cinnamoyl moiety (PubMed:33242032). The cytochrome P450 monooxygenase hkm5 catalyzes the methylenedioxy bridge formation, converting hancockiamide A into hancockiamide G (PubMed:33242032). Hkm5 can also convert hancockiamide B into hancockiamide C, and hancockiamide D into hancockiamide H (PubMed:33242032). The N- acetyltransferase hkm3 finally transfers an acetyl group to 1-N of piperazine, converting hancockiamide A into hancockiamide B and hancockiamide G into hancockiamide C (PubMed:33242032). SIMILARITY: Belongs to the tyrosinase family.


FUNCTION: Role in sperm cell division, maturation, or function. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 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 and as sensor of hydrogen peroxide-mediated signaling events. FUNCTION: Antioxidant. Could be involved in protection against reactive oxygen species (ROS) generated by metabolic processes and/or protection of the parasite against ROS released by immune effector cells. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.


FUNCTION: Mediates the nuclear localization of the ribonucleotide reductase. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DIF1/spd1 family.


FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. SIMILARITY: Belongs to the Nth/MutY family.


FUNCTION: Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May participate along with PAFAH1B1/LIS-1 in a distinct overlapping signaling pathway that promotes neuronal migration. SUBCELLULAR LOCATION: Cytoplasm Cell projection, neuron projection Note=Localizes at neurite tips.


FUNCTION: Involved in neuronal migration during development of the cerebral neocortex. May regulate the stability and proteasomal degradation of the estrogen receptors that play an important role in neuronal differentiation, survival and plasticity. Axonemal dynein assembly factor required for ciliary motility (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, neuron projection Dynein axonemal particle.


FUNCTION: Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication. SUBCELLULAR LOCATION: Virion Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus VP2 family.


SIMILARITY: Belongs to the FGGY kinase family.


FUNCTION: Probably binds the 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL4 family.


FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDK1, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. SIMILARITY: Belongs to the CND3 (condensin subunit 3) 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 Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL33 family.


FUNCTION: Transcription factor, which may be involved in the specification and maintenance of the stem cells (QC cells) in the root apical meristem (RAM). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family.


FUNCTION: Specifically methylates the N(7) position of guanine 1405 in 16S rRNA. Confers resistance to various aminoglycosides, including gentamicin and kanamycin. SIMILARITY: Belongs to the methyltransferase superfamily. Aminoglycoside resistance family.


FUNCTION: Transcriptional regulator. SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR family.


FUNCTION: Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (By similarity). Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.


FUNCTION: Involved in the secretion of harpin-pss; a proteinaceous elicitor of the hypersensitivity response in plants. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family.


FUNCTION: Transfers hydroxycinnamic moieties to the glucosyl groups of anthocyanin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the plant acyltransferase family.


FUNCTION: Member of the two-component regulatory system VraS/VraR involved in the control of the cell wall peptidoglycan biosynthesis. SUBCELLULAR LOCATION: Cytoplasm.


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


FUNCTION: Possesses similar cytotoxic and cytostimulatory activities to PRG2/MBP. SUBCELLULAR LOCATION: Note=Localized to the eosinophil secondary granule.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetokinase 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 betacoronaviruses E protein family.


FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein Note=Probably associates with membranes. SIMILARITY: Belongs to the VPS37 family.


FUNCTION: Probably plays an important role in intracellular peptide degradation (PubMed:20067529). FUNCTION: Probably plays an important role in intracellular peptide degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M17 family.


FUNCTION: In the presence of other necessary color factors, this glycosylation reaction allows the accumulation of anthocyanin pigments. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Target of p53/TP53 with pro-apoptotic function. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the complex I NDUFA3 subunit family.


FUNCTION: Capsid protein that self-associates to form pentons, building the capsid in association with hexamers of the major capsid protein and one dodecamer of the portal protein. SUBCELLULAR LOCATION: [Capsid vertex protein]: Virion. Note=Part of the capsid icosahedric shell of the immature virion. SIMILARITY: Belongs to the Tevenvirinae capsid vertex family.


FUNCTION: Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Voltage-insensitive potassium channel (PubMed:9628867). Channel opening is triggered by mechanical forces that deform the membrane. Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the sensory perception of pain caused by pressure (PubMed:19279663). Plays a role in the perception of pain caused by heat (PubMed:19279663). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the two pore domain potassium channel (TC 1.A.1.8) family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf20 family.


FUNCTION: Aspartic protease that processes the lipase LipY and other PE_PGRS proteins. Can also cleave itself. Cleaves LipY both inside the PE domain, before amino acid 98, and after amino acids 136 and 149. Involved in virulence. SUBCELLULAR LOCATION: Secreted Cell surface Note=Secreted via the ESX-5 / type VII secretion system (T7SS). SIMILARITY: Belongs to the mycobacterial PE family. PGRS subfamily.


FUNCTION: May be involved in proper membrane localization of Rab GTPases. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the YIP1 family.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Couples electron transfer from reduced ferredoxin to NAD(+) with electrogenic movement of Na(+) out of the cell. Involved in caffeate respiration. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily.


FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the UQCRH/QCR6 family.


FUNCTION: Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: May be an activator protein for the gylABX operon.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS7 family.


FUNCTION: The leader peptide is a component of released, infectious virions and is required for particle budding. FUNCTION: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to the cell receptor. This interaction triggers the refolding of transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). SUBCELLULAR LOCATION: [Envelope glycoprotein gp130]: Host endoplasmic reticulum membrane. Note=The polyprotein has a highly unusual biosynthesis for a retroviral glycoprotein. It is translated as a full- length precursor protein into the rough endoplasmic reticulum and initially has a type III protein configuration with both its N and C- termini located intracytoplasmically. SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein Host endoplasmic reticulum membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. SUBCELLULAR LOCATION: [Leader peptide]: Virion membrane; Single-pass type II membrane protein Host endoplasmic reticulum membrane; Single-pass type II membrane protein Note=Its N-terminus is located inside the viral particle. SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single-pass type I membrane protein.


FUNCTION: Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis. SIMILARITY: Belongs to the morbillivirus P protein family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Zeta family.


FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate. SIMILARITY: Belongs to the CobH/CbiC family.


SIMILARITY: Belongs to the DNA polymerase type-B family.


FUNCTION: A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis. SIMILARITY: Belongs to the YihI family.


FUNCTION: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily.


FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin (By similarity). Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Also binds the DEAR/FBXW7-AS1 receptor (By similarity). SIMILARITY: Belongs to the PDGF/VEGF growth factor family.


FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin- responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Aux/IAA family.


FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3438 (m5C3438) in 28S rRNA (PubMed:31722427). m5C3782 promotes protein translation without affecting ribosome biogenesis and fidelity (By similarity). Required for corpus callosum and cerebral cortex development (PubMed:31174389, PubMed:31462248). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.


SIMILARITY: Belongs to the GEM family.


FUNCTION: May participate in oleandomycin glycosylation and secretion during antibiotic production. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.


FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.


FUNCTION: Insecticidal neurotoxin that reversibly inhibits the N- methyl-D-aspartate (NMDA)-subtype of ionotropic glutamate receptor (GRIN) and inhibits inactivation of insect sodium channels (Nav). In vivo, is highly toxic to insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 05 subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ABC transporter superfamily.


SIMILARITY: Belongs to the glutamine synthetase family.


FUNCTION: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds (PubMed:32134669). FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners (PubMed:32134669). The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols (PubMed:32134669). In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products (PubMed:32134669). The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring (PubMed:32134669). The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners (PubMed:32134669). The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives (PubMed:32134669). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the LEA type 3 family.


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


FUNCTION: Structure-specific DNA-binding protein involved in DNA repair by promoting RAD51-mediated homologous recombination. Acts by stimulating D-Loop formation by RAD51: specifically enhances joint molecule formation through its structure-specific DNA interaction and its interaction with RAD51. Binds single-stranded DNA (ssDNA), double- stranded DNA (dsDNA) and secondary DNA structures, such as D-loop structures: has a strong preference for branched-DNA structures that are obligatory intermediates during joint molecule formation. Cooperates with WDR48/UAF1 to stimulate RAD51-mediated homologous recombination: both WDR48/UAF1 and RAD51AP1 have coordinated role in DNA-binding during homologous recombination and DNA repair. WDR48/UAF1 and RAD51AP1 also have a coordinated role in DNA-binding to promote USP1-mediated deubiquitination of FANCD2. Also involved in meiosis by promoting DMC1-mediated homologous meiotic recombination. SUBCELLULAR LOCATION: Chromosome Nucleus Chromosome, telomere Note=Colocalizes with RAD51 to multiple nuclear foci (PubMed:9192668, PubMed:21307306). Colocalizes with DMC1 on meiotic chromatin (PubMed:21307306).


FUNCTION: Probable transcription factor that acts downstream of egl-15, to promote migration of the HSN motor neurons from the tail to the gonad primordium during HSN cell differentiation (PubMed:10049362). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Member of 2 two-component regulatory system(s) Hik2/Rre1 and Hik2/RppA. Transduces PQ (plastoquinone) redox signals to photosystem gene expression machinery during the adjustment of photosystem stoichiometry. Reduced PQ suppresses its autophosphorylation activity (i.e. kinase activity is higher under oxidizing conditions). As part of a two-component regulatory system with Rre1, controls expression of sigB and several other genes in response to hyperosmotic stress. May transfer phosphate to RppA in a possible Hik2/RppA two-component system. SIMILARITY: Belongs to the chloroplast sensor kinase protein family.


SIMILARITY: Belongs to the Mo25 family.


FUNCTION: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family.


FUNCTION: Plays a role in the control of cell shape and motility in the trabecular meshwork. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.


FUNCTION: Required for genome encapsidation. Forms ribonucleoprotein complexes along with TGB1 helicase and viral RNA. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the potexviruses coat protein family.


FUNCTION: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ). SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.


FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (PubMed:10578051). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain- lengths of C8-C18 (PubMed:10578051). May play an important physiological function in brain (PubMed:10578051). SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytosol.


FUNCTION: Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the MAF1 family.


FUNCTION: Required for normal plant development (PubMed:17339883, PubMed:17932459, PubMed:18227644). Required for pollen germination (PubMed:17339883, PubMed:17259285, PubMed:18227644). Required for autophagic activity. Required to limit the pathogen-associated cell death response (PubMed:17932459). May be involved in vacuolar protein sorting (PubMed:17259285). Binds to microtubules. May facilitate efficient recruitment of other ATG proteins to assemble scaffolds for autophagosome biogenesis (PubMed:26566764). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Note=Colocalizes with ATG8I in punctuate structures (PubMed:17259285). Localizes in punctuate structures and colocalizes with microtubules (PubMed:26566764). SIMILARITY: Belongs to the beclin family.


FUNCTION: 3'-5' DNA helicase that may play a role in the repair of DNA (PubMed:18419780, PubMed:19755539). Its DNA unwinding activity in vitro is dependent on magnesium, and ATP or dATP (PubMed:18419780, PubMed:19755539). Can use GTP/dGTP, CTP/dCTP or UTP/dUTP as nucleotide cofactors (PubMed:18419780, PubMed:19755539). Catalyzes Holliday junction branch migration and replication fork regression (PubMed:19755539, PubMed:23771268). Disrupts D-loop structures (PubMed:18419780). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the helicase family. RecQ subfamily.


FUNCTION: Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt- dependent activation of FZD4, suggesting the existence of a Wnt- independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP- dependent cleavage activity. FUNCTION: Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt- dependent activation of FZD4, suggesting the existence of a Wnt- independent signaling that also promote accumulation the beta-catenin (CTNNB1). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family.


FUNCTION: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal (PubMed:15548601, PubMed:15637057, PubMed:17478547, PubMed:19594707, PubMed:20130089). Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol (PubMed:15548601, PubMed:15637057, PubMed:17478547, PubMed:19594707, PubMed:20130089). Cargo protein-binding triggers interaction with PEX5 and formation of a ternary complex composed of PEX5 and PEX7 along with PTS2-containing cargo proteins, which is tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex (PubMed:15548601, PubMed:15637057, PubMed:17478547, PubMed:19594707, PubMed:20130089). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome matrix Note=The loss of PEX12, PEX13 or PEX14 prevents the targeting of PEX7 to peroxisomes. SIMILARITY: Belongs to the WD repeat peroxin-7 family.


FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB (By similarity). FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm.


SIMILARITY: Belongs to the acetolactate synthase small subunit family.


FUNCTION: Intracellular channel initially characterized as a non- selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a voltage-gated highly- selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate) that senses pH changes and confers electrical excitability to organelles (PubMed:19620632, PubMed:23063126, PubMed:24776928, PubMed:23394946). Localizes to the early and recycling endosomes membranes where it plays a role in the uptake and processing of proteins and regulates organellar membrane excitability, membrane trafficking and pH homeostasis (PubMed:23394946) (Probable). Ion selectivity is not fixed but rather agonist-dependent and under defined ionic conditions, can be readily activated by both NAADP and PI(3,5)P2 (Probable). Required for mTOR-dependent nutrient sensing (PubMed:23394946) (Probable). FUNCTION: (Microbial infection) During Ebola virus (EBOV) infection, controls the movement of endosomes containing virus particles and is required by EBOV to escape from the endosomal network into the cell cytoplasm. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC 1.A.1.11) family. Two pore calcium channel subfamily.


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


FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Sigma 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. uS11 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS11 family.


FUNCTION: Catalyzes the final step in the CDP-choline route leading to phosphatidylcholin (PC). Preferentially uses CDP-monomethylethanolamine as aminoalcohol substrate. Shows highest activity toward di- and mono- unsaturated diacylglycerol species as lipid substrates. The CDP-choline pathway only contributes to net PC synthesis if exogenous choline is present. In its absence, this pathway recycles choline from PC turnover and may contribute to maintaining the proper PC species composition. SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family.


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


FUNCTION: Binds 5 molecules of zinc. May have a role in Zn(2+) homeostasis during embryogenesis. SIMILARITY: Belongs to the metallothionein superfamily. Type 15 family.


SIMILARITY: Belongs to the UPF0162 family.


FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. SIMILARITY: Belongs to the proteasome subunit S3 family.


FUNCTION: Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-I subfamily.


FUNCTION: Antimicrobial peptide. Active against Gram-negative bacterium E.coli (MIC=12.5 uM) and against Gram-positive bacterium S.aureus (MIC=12.5 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.


FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane.


FUNCTION: [Antibacterial peptide LL-37]: Antimicrobial peptide that is an integral component of the innate immune system (By similarity). Binds to bacterial lipopolysaccharides (LPS) (By similarity). Causes membrane permeabilization by forming transmembrane pores (in vitro) (By similarity). Causes lysis of E.coli (By similarity). Exhibits antimicrobial activity against Gram-negative bacteria such as P.aeruginosa, S.typhimurium, E.aerogenes, E.coli and P.syringae, Gram- positive bacteria such as L.monocytogenes, S.epidermidis, S.pyogenes and S.aureus, as well as vancomycin-resistant enterococci (in vitro) (By similarity). Exhibits antimicrobial activity against methicillin- resistant S.aureus, P.mirabilis, and C.albicans in low-salt media, but not in media containing 100 mM NaCl (in vitro) (By similarity). Forms chiral supramolecular assemblies with quinolone signal (PQS) molecules of P.aeruginosa, which may lead to interference of bacterial quorum signaling and perturbance of bacterial biofilm formation (By similarity). May form supramolecular fiber-like assemblies on bacterial membranes (By similarity). Induces cytokine and chemokine producation as well as TNF/TNFA and CSF2/GMCSF production in normal human keratinocytes (By similarity). Exhibits hemolytic activity against red blood cells (By similarity). FUNCTION: [Antibacterial peptide FALL-39]: Exhibits antimicrobial activity against E.coli and B.megaterium (in vitro). FUNCTION: Antimicrobial protein that is an integral component of the innate immune system (By similarity). Binds to bacterial lipopolysaccharides (LPS) (By similarity). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (By similarity). Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (By similarity). The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram- negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (By similarity). SUBCELLULAR LOCATION: Secreted Vesicle Note=Stored as pro-peptide in granules and phagolysosomes of neutrophils (By similarity). Secreted in sweat onto skin (By similarity). SIMILARITY: Belongs to the cathelicidin family.


FUNCTION: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched- chain alpha-ketoacids to acyl-CoA and CO(2). FUNCTION: Component of the branched-chain alpha-ketoacid dehydrogenase (BCKADH) complex, that catalyzes the overall conversion of branched- chain alpha-ketoacids to acyl-CoA and CO(2).


FUNCTION: Metalloglycoprotein, containing Ca, Mg, Mn, and Zn and the carbohydrates galactose, glucosamine, mannose, and fucose. It agglutinates erythrocytes of blood group A1. SIMILARITY: Belongs to the leguminous lectin family.


FUNCTION: Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). SUBCELLULAR LOCATION: Membrane; Lipid-anchor Cytoplasm Microsome Mitochondrion Nucleus Cytoplasm, perinuclear region Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity).


FUNCTION: Probable secreted effector that may act as a pathogen- associated molecular pattern (PAMP) recognized by the plant immune system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Necrosis inducing protein (NPP1) family.


FUNCTION: Vesicle trafficking protein that functions in the secretory pathway. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the novel plant SNARE family.


FUNCTION: Deubiquitinating enzyme that cleaves both 'Lys-48'-linked and 'Lys-63'-linked poly-ubiquitin chains (in vitro). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol- anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGV family.


FUNCTION: When expressed in E.coli with Synechocystis PhaC and C.necator PhaA and PhaB, confers the ability to synthesize up to 13% (w/w) poly(3-hydroxybutyrate) (PHB) depending on the carbon source; all 4 genes are necessary for PHB production (PubMed:9683655). Cell-free in vitro coexpression with PhaE gives a heterodimer able to polymerize 3- hydroxybutyrate-CoA (PubMed:25629766). This subunit has no catalytic activity but enhances the activity of PhaC, the catalytic subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PHA/PHB synthase family. Type III PhaE subfamily.


FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Contributes to the regulation of the fast action potential repolarization and in sustained high-frequency firing in neurons of the central nervous system (PubMed:10561420, PubMed:10414303, PubMed:11124984, PubMed:10903572, PubMed:11506885, PubMed:15317859, PubMed:15917463, PubMed:17761775, PubMed:21414897). Homotetramer channels mediate delayed-rectifier voltage-dependent potassium currents that activate rapidly at high-threshold voltages and inactivate slowly (PubMed:10414303). Forms tetrameric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (By similarity). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNC1, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:10531438, PubMed:12000114). Channel properties may be modulated by either the association with ancillary subunits, such as KCNE1, KCNE2 and KCNE3 or indirectly by nitric oxide (NO) through a cGMP- and PKG-mediated signaling cascade, slowing channel activation and deactivation of delayed rectifier potassium channels (By similarity). Contributes to fire sustained trains of very brief action potentials at high frequency in thalamocortical and suprachiasmatic nucleus (SCN) neurons, in hippocampal and neocortical interneurons and in retinal ganglion cells (PubMed:10561420, PubMed:10903572, PubMed:11506885, PubMed:17761775). Sustained maximal action potential firing frequency in inhibitory hippocampal interneurons is negatively modulated by histamine H2 receptor activation in a cAMP- and protein kinase (PKA) phosphorylation- dependent manner (PubMed:10903572). Plays a role in maintaining the fidelity of synaptic transmission in neocortical GABAergic interneurons by generating action potential (AP) repolarization at nerve terminals, thus reducing spike-evoked calcium influx and GABA neurotransmitter release (PubMed:15917463). Required for long-range synchronization of gamma oscillations over distance in the neocortex (PubMed:22539821). Contributes to the modulation of the circadian rhythm of spontaneous action potential firing in suprachiasmatic nucleus (SCN) neurons in a light-dependent manner (PubMed:21414897). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Membrane; Multi-pass membrane protein Perikaryon Cell projection, axon Cell projection, dendrite Postsynaptic cell membrane Presynaptic cell membrane Synapse, synaptosome Synapse Apical cell membrane Basolateral cell membrane Note=Colocalizes with parvalbumin in globus pallidus neurons. Localizes in thalamocortical axons and synapses (By similarity). Localizes on the surface of cell somata, proximal dendrites and axonal membranes (PubMed:12000114, PubMed:10903572). Also detected throughout the neuropil (PubMed:12000114). Localized in starburst cell somata and proximal dendrite processes (PubMed:15317859). Colocalized with GABA in presynaptic terminals (PubMed:10531438). Clustered in patches in somatic and proximal dendritic membrane as well as in axons and presnypatic terminals of GABAergic interneurons; some of these patches are found near postsynaptic sites (PubMed:10531438). SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC 1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily.


FUNCTION: May be involved in the brassinosteroids (BRs) signaling pathway and regulate the growth and development of rosette leaves (PubMed:28887625). Seems to prevent over development of leaves and inflorescence stems (PubMed:12012249). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RING-type zinc finger family.


FUNCTION: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position. SIMILARITY: Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily.


FUNCTION: Catalyzes the 3-beta-hydroxylation of the inactive gibberellin precursors, leading to the formation of bioactive gibberellins. In vitro, converts the precursors GA20, GA5, GA44 and GA9 to the corresponding 3-beta-hydroxylated active products GA1, GA3, GA38 and GA4, respectively. Involved in the production of bioactive GA for vegetative growth and development (PubMed:11438692). Controls the elongation of the vegetative shoot and plant height by the regulation of active gibberellin levels (Ref.7). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.


FUNCTION: Phosphatase with a broad specificity. Its primary physiological function is to dephosphorylate 3'-phosphoadenosine 5'- phosphate (PAP) and 3'-phosphoadenosine 5'-phosphosulfate (PAPS). Thus, plays a role in mycobacterial sulfur metabolism, since it can serve as a key regulator of the sulfate assimilation pathway by controlling the pools of PAP and PAPS in the cell. To a lesser extent, is also able to hydrolyze inositol 1-phosphate (I-1-P), fructose 1,6-bisphosphate (FBP) (to fructose 6-phosphate (F-6-P)) and AMP in vitro, but this might not be significant in vivo (By similarity). SIMILARITY: Belongs to the inositol monophosphatase superfamily.


FUNCTION: Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11081638). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:11081638). Also activated by phorbol esters (PubMed:19864432). Channel activity seems to be regulated by a calmodulin-dependent mechanism (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cell junction, adherens junction. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV4 sub-subfamily.


FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Phe). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily.


FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1A family.


FUNCTION: Sesquiterpene cyclase catalyzing the production of sixfold more beta-farnesene than alpha-bergamotene from farnesyl diphosphate. Involved in indirect defense by producing volatile signals attracting natural enemies of herbivores. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Member of the two-component regulatory system BvgS/BvgA. Activates the transcription of virulence genes.


FUNCTION: Probable antitoxin component of a type II toxin-antitoxin (TA) system. The cognate toxin is VapC5. FUNCTION: Probable antitoxin component of a probable type II toxin- antitoxin (TA) system. The cognate toxin is VapC5 (By similarity). SIMILARITY: Belongs to the phD/YefM antitoxin family.


SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family.


FUNCTION: E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity). May be involved in T-cell proliferation by regulating LIF secretion (By similarity). May play a role in lysosome homeostasis (By similarity).


FUNCTION: Cleaves the 2'-5' phosphodiester linkage at the branch point of lariat intron pre-mRNAs after splicing and converts them into linear molecules that are subsequently degraded. It thereby facilitates ribonucleotide turnover. It may also participate in retrovirus replication via an RNA lariat intermediate in cDNA synthesis. Plays en essential role during embryogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the lariat debranching enzyme family.


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


FUNCTION: Forms a water channel with a broad specificity. Also permeable glycerol and urea. Mediates passage of a wide variety of small, non-charged solutes including carbamides, polyols, purines, and pyrimidines. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.


FUNCTION: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity). SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the peptidase S10 family.


FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family.


FUNCTION: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs. Requires a tRNA-binding adapter protein for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (Probable). Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility (PubMed:11493925). 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 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RNA cytidine acetyltransferase family. NAT10 subfamily.


FUNCTION: Phagocytic receptor, strong negative regulator of T-cell proliferation and IL2 production. Potent inhibitor of the alternative complement pathway convertases. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Involved in acetylcholine transport into synaptic vesicles. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Vesicular transporter family.


SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family.


FUNCTION: Sesquiterpene synthase. SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.


FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation- dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'- 3' cyclic phosphate termini. Cmr4 is probably the subunit that cleaves target RNA (PubMed:25280103). Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CRISPR system Cmr3 family.


FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity). SIMILARITY: Belongs to the serine/threonine dehydratase family.


FUNCTION: Involved in melatonin degradation (PubMed:25728912). Catalyzes the hydroxylation of melatonin to produce 2-hydroxymelatonin (PubMed:25728912). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.


FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex NUBP1-NUBP2. Electrons are transferred to CIAPIN1 from NADPH via the FAD- and FMN-containing protein NDOR1. NDOR1-CIAPIN1 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion intermembrane space. SIMILARITY: Belongs to the anamorsin family.


FUNCTION: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons (By similarity). Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity). SUBCELLULAR LOCATION: Spore membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WTF family.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A- phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PTPA-type PPIase family.


FUNCTION: May play a role in lipid transport protein in Schwann cells. May bind cholesterol. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.


FUNCTION: Snake phospholipase A2 homolog that lacks enzymatic activity (PubMed:19944711, PubMed:20036276). May display myotoxin activity (Probable). In isolated heart decreases cardiac frequency (PubMed:20036276). Also decreases mean arterial pressure (PubMed:19944711). Does not show antimicrobial activity (PubMed:19944711). Does not change renal parameters (such as perfusion pressure, renal vascular resistance, urinary flow, glomerular filtration rate and sodium tubular transport) (PubMed:20036276). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily.


FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin- protein ligase and modulates its activity. Sequesters tumor suppressor TP53 in the host cytoplasm and modulates its activity by interacting with host EP300 that results in the reduction of TP53 acetylation and activation. In turn, apoptosis induced by DNA damage is inhibited. E6 protects also host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the papillomaviridae E6 protein family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.


FUNCTION: May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein. Synapse. Note=Synaptic vesicles in neurons. SIMILARITY: Belongs to the synaptotagmin family.


FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrF/TusC family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.


FUNCTION: Facilitates ubiquitin-independent proteasomal degradation of polycomb protein CBX4. Plays a role in inhibiting the activity of glucokinase GCK and both glucose-induced and basal insulin secretion. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Nucleus, nucleolus Note=Detected in the nucleus and nucleolus with no expression in the cytoplasm. However, a later study finds expression in the nucleus and cytoplasm with no expression in the nucleolus.


FUNCTION: Component of the ASTRA complex involved in chromatin remodeling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat ASA1 family.


FUNCTION: Potential regulator of CDK5 activity. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily.


FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase family. Thioredoxin-coupled ArsC subfamily.


SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase family.


FUNCTION: Required for ciliogenesis. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Cell projection, cilium Note=Localizes to vesicles en route to the base of cilium. SIMILARITY: Belongs to the TMEM138 family.


FUNCTION: GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. Ran family.


FUNCTION: Regulator of autophagy that contributes to antagonize becn1- mediated cellular autophagy at the endoplasmic reticulum. Participates in the interaction of bcl2 with becn1 and is required for bcl2-mediated depression of endoplasmic reticulum Ca(2+) stores during autophagy (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CISD protein family. CISD2 subfamily.


FUNCTION: FliN is one of three proteins (FliG, FliN, FliM) that form 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 membrane; Peripheral membrane protein; Cytoplasmic side Bacterial flagellum basal body. SIMILARITY: Belongs to the FliN/MopA/SpaO family.


FUNCTION: Hydrolyzes the ester bond of the acyl group attached at the sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1- acyl-2-lysophosphatidylserines (lysophospholipase activity) in the pathway of phosphatidylserines acyl chain remodeling (PubMed:8999922). Cleaves phosphatidylserines exposed on the outer leaflet of the plasma membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines, which in turn enhance mast cell activation and histamine production (PubMed:11395520). Has no activity toward other glycerophospholipids including phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or phosphatidylinositols, or glycerolipids such as triolein (PubMed:8999922). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (- COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.


SIMILARITY: Belongs to the BolA/IbaG family.


FUNCTION: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.


FUNCTION: Involved in the apoptotic response after nerve growth factor (NGF) binding in neuronal cells. Inhibits cell cycle progression, and facilitates NGFR-mediated apoptosis. May act as a regulator of the function of DLX family members. May enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. Proposed to act through recruitment and/or stabilization of the Ubl- conjugating enzyme (E2) at the E3:substrate complex. Plays a role in the circadian rhythm regulation. May act as RORA coregulator, modulating the expression of core clock genes such as BMAL1 and NFIL3, induced, or NR1D1, repressed. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane; Peripheral membrane protein Note=Expression shifts from the cytoplasm to the plasma membrane upon stimulation with NGF.


SIMILARITY: Belongs to the TTC39 family.


FUNCTION: RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. May regulate ProP activity through an RNA-based, post-transcriptional mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ProQ 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. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPC7 RNA polymerase subunit family.


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


FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family. SIMILARITY: Belongs to the FlgH family.


FUNCTION: Pro-inflammatory cytokine involved in the innate immune response to bacterial pathogens. The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense. Counteracts the anti-inflammatory activity of glucocorticoids. Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known. It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity. SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Does not have a cleavable signal sequence and is secreted via a specialized, non- classical pathway. Secreted by macrophages upon stimulation by bacterial lipopolysaccharide (LPS), or by M.tuberculosis antigens. SIMILARITY: Belongs to the MIF family.


FUNCTION: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with tom20 and tom22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the tom40 translocation pore. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Tom70 family.


SIMILARITY: Belongs to the lysopine/nopaline/octopine/opine/vitopine dehydrogenases family.


FUNCTION: Pectinolytic enzyme that degrades type I rhamnogalacturonan from plant cell walls and releases oligosaccharide products (PubMed:16682770, PubMed:17449691, PubMed:19193638). Degrades rhamnogalacturonan, polygalacturonic acid, pectic acid and pectin (PubMed:16682770, PubMed:17449691). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 11 family.


FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. SIMILARITY: Belongs to the glycosyl hydrolase 35 family.


FUNCTION: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


SUBCELLULAR LOCATION: Endoplasmic reticulum.


FUNCTION: May bind to both alpha-IIb/beta-3 (ITGA2B/ITGB3) and alpha- V/beta-3 (ITGAV/ITGB3) integrins, and may inhibit platelet aggregation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the disintegrin family. Dimeric disintegrin subfamily.


FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role in ciliogenesis (By similarity). SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. SUBCELLULAR LOCATION: [Isoform 1]: Secreted. SIMILARITY: Belongs to the villin/gelsolin family.


FUNCTION: Voltage-gated ATP nucleotide uniporter that can also transport the purine nucleotides ADP and GTP. Uses the membrane potential as the driving force to control ATP accumulation in lysosomes and secretory vesicles (PubMed:18375752, PubMed:23467297). By controlling ATP storage in lysosomes, regulates ATP-dependent proteins of these organelles (PubMed:35269509). Also indirectly regulates the exocytosis of ATP through its import into lysosomes in astrocytes and secretory vesicles such as adrenal chromaffin granules, mucin granules and synaptic vesicles (PubMed:18375752, PubMed:23467297). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane; Multi-pass membrane protein Cytoplasmic vesicle, secretory vesicle membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Note=Localizes to mucin granules and vesicles. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family.


FUNCTION: Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.


FUNCTION: Component of the DSC E3 ubiquitin ligase complex which is required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. The complex also plays an important role in the multivesicular body (MVB) pathway and functions in a post- endoplasmic reticulum pathway for protein degradation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein.


FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.


FUNCTION: Evokes contractions in the radula protractor muscle, and may regulate feeding behavior and gut motility by controlling muscle contraction of the buccal mass. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SCP family.


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


SIMILARITY: Belongs to the mite group 5 allergen family.


FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that promotes disulfide bond formation in client proteins through its thiol- disulfide oxidase activity. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.


FUNCTION: Has antifungal activity. Inhibits the growth of Trichoderma viridae and Candida albicans. SIMILARITY: Belongs to the thaumatin family.


FUNCTION: Not known. Could enhance the incorporation of nickel to the hydrogenase. SIMILARITY: Belongs to the HupH/HyaF family.


FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Can also catalyze the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4- hydroxy-D-proline (c4DHyp), albeit with 30-fold lower efficiency. Is likely involved in both degradation pathways that convert t3LHyp to L- proline and t4LHyp to alpha-ketoglutarate, which would allow A.tumefaciens to grow on t3LHyp or t4LHyp as a sole carbon source. Displays no proline racemase activity. SIMILARITY: Belongs to the proline racemase family.


FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line Note=Colocalizes with Smn at the Z-line of indirect flight muscles. SIMILARITY: Belongs to the alpha-actinin family.


FUNCTION: Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase S54 family.


FUNCTION: Involved in vacuolar protein sorting. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the VPS62 family.


FUNCTION: Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophosphatidylinositol (1- acylglycerophosphatidylinositol or LPI) leading to the production of a phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI) and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle (PubMed:18772128, PubMed:18094042). Prefers arachidonoyl-CoA as the acyl donor, thus contributing to the regulation of free levels arachidonic acid in cell (PubMed:18772128, PubMed:18094042). In liver, participates in the regulation of triglyceride metabolism through the phosphatidylinositol acyl-chain remodeling regulation (PubMed:32253259). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localized in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria. SIMILARITY: Belongs to the membrane-bound acyltransferase family.


FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.


FUNCTION: Inhibits voltage-gated potassium channels (Kv) with higher potency for Kv1.1/KCNA1 and Kv1.3/KCNA3. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin family. Type 1a subfamily.


FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Antp homeobox family. Labial subfamily.


FUNCTION: Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. May also play a role in infection by viruses through mechanisms that may involve chromatin and/or transcriptional regulation (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, PML body Nucleus, nuclear body Cytoplasm Note=Accumulates in the cytoplasm upon FAS activation.


FUNCTION: Probable molecular chaperone assisting protein biosynthesis and transport in the endoplasmic reticulum (PubMed:16433634, PubMed:28939891). Required for the proper biosynthesis and transport of pulmonary surfactant-associated protein A/SP-A, pulmonary surfactant- associated protein D/SP-D and the lipid transporter ABCA3 (By similarity). By regulating both the proper expression and the degradation through the endoplasmic reticulum-associated protein degradation pathway of these proteins plays a crucial role in pulmonary surfactant homeostasis (By similarity). Has an anti-fibrotic activity by negatively regulating the secretion of type I and type III collagens (PubMed:28939891). This calcium-binding protein also transiently associates with immature PCSK6 and regulates its secretion (PubMed:16433634). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the CREC family.


FUNCTION: Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 (By similarity). FUNCTION: Structural peptide 2 is a small peptide derived from pVP2 C- terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity). FUNCTION: Capsid protein VP3 plays a key role in virion assembly by providing a scaffold for the capsid made of VP2. May self-assemble to form a T=4-like icosahedral inner-capsid composed of at least 180 trimers. Plays a role in genomic RNA packaging by recruiting VP1 into the capsid and interacting with the dsRNA genome segments to form a ribonucleoprotein complex. Additionally, the interaction of the VP3 C- terminal tail with VP1 removes the inherent structural blockade of the polymerase active site. Thus, VP3 can also function as a transcriptional activator (By similarity). FUNCTION: Structural peptide 3 is a small peptide derived from pVP2 C- terminus. It is not essential for the virus viability, but viral growth is affected when missing (By similarity). FUNCTION: Structural peptide 1 is a small peptide derived from pre-VP2 C-terminus. It destabilizes and perforates cell membranes, suggesting a role during entry (By similarity). FUNCTION: The precursor of VP2 plays an important role in capsid assembly. First, pre-VP2 and VP2 oligomers assemble to form a procapsid. Then, the pre-VP2 intermediates may be processed into VP2 proteins by proteolytic cleavage mediated by VP4 to obtain the mature virion. The final capsid is composed of pentamers and hexamers but VP2 has a natural tendency to assemble into all-pentameric structures. Therefore pre-VP2 may be required to allow formation of the hexameric structures (By similarity). FUNCTION: Protease VP4 is a serine protease that cleaves the polyprotein into its final products. Pre-VP2 is first partially cleaved, and may be completely processed by VP4 upon capsid maturation. FUNCTION: Structural peptide 4 is a small peptide derived from pVP2 C- terminus. It is essential for the virus viability (By similarity). SUBCELLULAR LOCATION: [Structural peptide 4]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Structural peptide 2]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Structural peptide 3]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion Host cytoplasm. SUBCELLULAR LOCATION: [Structural peptide 1]: Virion Host cytoplasm.


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. Microtubule inner protein (MIP) part of the dynein- decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (PubMed:34715025). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the NDK family.


FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.


FUNCTION: The first domain inhibits trypsin; the second one inhibitis subtilisin.


FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.


SIMILARITY: To E.coli YcjX.


FUNCTION: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8- ribityllumazine, resulting in the formation of riboflavin and 5-amino- 6-(D-ribitylamino)uracil.


FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type II-A(UA) CBASS system (PubMed:32839535). FUNCTION: Cyclic dinucleotide synthase that catalyzes the synthesis of 3',3'-cyclic UMP-AMP (cUMP-AMP) from UTP and ATP, a second messenger for cell signal transduction. Controls the activity of cUAMP-activated phospholipase CapE, a patatin-like lipase that is a direct cUMP-AMP receptor encoded in the cdnE operon. SIMILARITY: Belongs to the CD-NTase family. E01 subfamily.


SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endophilin 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. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participates in regulation of intracellular nucleotide homeostasis. Binds to anionic phospholipids, predominantly to cardiolipin; the binding inhibits its phosphotransfer activity. Acts as mitochondria-specific NDK; its association with cardiolipin-containing mitochondrial inner membrane is coupled to respiration suggesting that ADP locally regenerated in the mitochondrion innermembrane space by its activity is directly taken up via ANT ADP/ATP translocase into the matrix space to stimulate respiratory ATP regeneration. Proposed to increase GTP-loading on dynamin-related GTPase OPA1 in mitochondria. In vitro can induce liposome cross-linking suggesting that it can cross-link inner and outer membranes to form contact sites, and promotes intermembrane migration of anionic phosphoplipids. Promotes the redistribution of cardiolipin between the mitochondrial inner membrane and outer membrane which is implicated in pro-apoptotic signaling (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space; Peripheral membrane protein. Mitochondrion matrix Note=Predominantly localized in the mitochondrion intermembrane space. Colocalizes with OPA1 in mitochondria (By similarity). SIMILARITY: Belongs to the NDK family.


FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. SIMILARITY: Belongs to the acetokinase family. TdcD subfamily.


FUNCTION: May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo- dGTP to the monophosphate (By similarity). FUNCTION: May be involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo- dGTP to the monophosphate (By similarity). In vitro has 8-oxo-dGTPase activity. SIMILARITY: Belongs to the Nudix hydrolase family.


FUNCTION: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS and DLG4/PSD95. SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor; Cytoplasmic side Cell projection, dendritic spine Postsynaptic density membrane. SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD17 family.