FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. Degrades antitoxin MazE (PubMed:24375411). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S14 family.


FUNCTION: Snake venom zinc metalloproteinase that inhibits ADP-induced platelet aggregation (probably by binding integrin alpha-IIb/beta-3 (ITGA2B/ITGB3)) and degrades fibrinogen. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIb sub-subfamily.


FUNCTION: A tubulin-like, filament forming GTPase; the motor component of the type III plasmid partition system which ensures correct segregation of the pBCXO1 plasmid. It is essential for plasmid replication (By similarity). Binds GTP and forms filaments. The filaments seed from a DNA centromere-like site (tubC)-TubR complex which extends to surround the TubZ filaments. Highly dynamic filaments grow at the plus end and depolymerize at the minus end, a process called treadmilling. TubR-tubC complexes track the depolymerizing minus end of the filament, probably pulling plasmid within the cell (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Forms long, dynamic filaments. SIMILARITY: Belongs to the FtsZ family. TubZ subfamily.


SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane protein.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.


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


FUNCTION: Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LPG synthase family.


FUNCTION: Involved in the production of citral, a mixture of geranial and neral with a strong lemony scent. Reversibly oxidizes geraniol and nerol in equal efficiency. Also active, although at a lower efficiency, with cinnamyl alcohol. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Transcription factor, which in cooperation with EMX2, acts to generate the boundary between the roof and archipallium in the developing brain. May function in combinations with OTX1/2 to specify cell fates in the developing central nervous system (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EMX homeobox family.


SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Mitochondrial E3 ubiquitin-protein ligase that plays a crucial role in the control of mitochondrial morphology by acting as a positive regulator of mitochondrial fission. May play a role in the prevention of cell senescence acting as a regulator of mitochondrial quality control. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: Isomerase that catalyzes the condensation of two molecules of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine ring system. The final product is not yet known. SIMILARITY: Belongs to the PhzF family.


FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G- 3' consensus core sequence. SUBCELLULAR LOCATION: Nucleus.


SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.


FUNCTION: May promote plant stress tolerance (By similarity). Galactinol synthase mainly involved in the biosynthesis of transport raffinose family oligosaccharides (RFOs) that function as osmoprotectants. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyltransferase 8 family. Galactosyltransferase subfamily.


FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the ORC5 family.


FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. FUNCTION: Does not show activity on the acetylcholine receptors tested. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily.


FUNCTION: Putative receptor protein kinase. Could play a role in a differentiation signal. The CRINKLY4 (CR4) mutation affects leaf epidermis differentiation such that cell size and morphology are altered, and surface functions are compromised, allowing graft-like fusions between organs. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endosome, multivesicular body membrane; Single-pass type I membrane protein Note=Also localized into protein export bodies. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Cleaves host elastase, collagen, IgI and several complement components as well as endogenous pro-aminopeptidase, pro-chitin-binding protein (cbpD). Cleaves its own pro-peptide. Involved in the pathogenesis of P.aeruginosa infections. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family.


FUNCTION: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 03 subfamily.


FUNCTION: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth. SUBCELLULAR LOCATION: Lipid droplet. Membrane; Multi-pass membrane protein. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. SIMILARITY: Belongs to the oleosin family.


FUNCTION: Plays a role in the inhibition of host innate immune response. Within the host nucleus, inhibits activation of interferon- beta promoter by inhibiting IRF3 activation. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the poxviridae OPG036 family.


FUNCTION: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins subfamily. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (By similarity). This sigma factor is involved in regulation of cellulosomal genes via an external polysaccharide-sensing mechanism (Probable). Recognizes the predicted promoters associated with sigI3 itself, pl11, ce12 and cipA (PubMed:26731480). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. SigI subfamily.


FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By similarity). FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.


FUNCTION: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Regulates drug efflux through modulation of ABCB1 localization and activity. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.


FUNCTION: Receptor for retinoic acid that acts as a transcription factor. Forms homo- or heterodimers with retinoic acid receptors (rars) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription. The high affinity ligand for rxrs is 9-cis retinoic acid. In the absence of ligand, the rar/rxr heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily.


FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus (By similarity). SUBCELLULAR LOCATION: Lysosome Melanosome.


FUNCTION: NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. May play a role in the regulation of molting. Has lower activity with phenylglyoxal and isatin (in vitro). Has no activity with NADH as cosubstrate. Has no activity with nitrobenzaldehyde and 3-hydroxybenzaldehyde. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Implicated in a number of adherence functions. OPA proteins are implicated in pathogenesis and are subject to phase variation. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the opacity porin family.


FUNCTION: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection (PubMed:23377181, PubMed:25387135, PubMed:30595554). Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4 (PubMed:30595554). Inhibits the host salicylic acid pathway during infection (PubMed:25387135). SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.


FUNCTION: Positively regulates a late step in synaptic vesicle exocytosis. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SIMILARITY: Belongs to the complexin/synaphin family.


FUNCTION: This enzyme is a serine protease capable of degrading the native triple helix of collagen. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Inhibitor that slows proliferation of secreting cells (also known as chalone). Requires aprA for activity. SUBCELLULAR LOCATION: Secreted Note=Concentrated in subcellular structures, possibly vesicles. SIMILARITY: Belongs to the peptidase C1 family.


FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3- phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HAD-like hydrolase superfamily.


SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein Host cell surface. SIMILARITY: Belongs to the orthopoxvirus OPG172 protein family.


FUNCTION: Binds to site 3 of voltage-gated sodium channels and inhibits the inactivation process (PubMed:18538344). Is highly active on DmNav1/TipE (drosophila) and is only extremely weakly active on rat Nav1.4-beta-1/SCN4A-SCN1B, and on human Nav1.5-beta-1/SCN5A-beta-1 (PubMed:18538344). This reveals high specificity for arthropod over mammalian channels (PubMed:18538344). In vivo, when released into the medium, this recombinant toxin induces impaired swimming, paralysis and death of the crustacean A.nauplii within several hours (PubMed:22048953). Also causes paralysis of cherry shrimps immediately after injection at very low doses (PubMed:29424690). Its effect on zebrafish (D.rerio) larvae is also rapid, since it induces tail twitching accompanied by impaired swimming after 20 minutes and complete paralysis within 45 minutes (PubMed:22048953). It has also been observed to cause death of zebrafish larvae within 1 hour (PubMed:31134275). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type II subfamily.


FUNCTION: Reduces the C14=C15 double bond of 4,4-dimethyl-cholesta- 8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERG4/ERG24 family.


FUNCTION: Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto- oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box. SIMILARITY: Belongs to the MalT family.


FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions (By similarity). Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb (By similarity). Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP (By similarity). Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapes in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction (By similarity). In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation (By similarity). Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1 (By similarity). SUBCELLULAR LOCATION: [Amyloid-beta protein 42]: Cell surface Note=Associates with FPR2 at the cell surface and the complex is then rapidly internalized. SUBCELLULAR LOCATION: [Gamma-secretase C-terminal fragment 59]: Nucleus Cytoplasm Note=Located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). In dopaminergic neurons, the phosphorylated form is localized to the nucleus (By similarity). SUBCELLULAR LOCATION: [Soluble APP-beta]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane; Single-pass type I membrane protein Perikaryon Cell projection, growth cone Membrane, clathrin-coated pit Early endosome Cytoplasmic vesicle Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. Only a minor proportion is present at the cell membrane; most of the protein is present in intracellular vesicles. During maturation, the immature APP (N- glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. SIMILARITY: Belongs to the APP family.


FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). SIMILARITY: Belongs to the ELP3 family.


FUNCTION: Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TNF receptor-associated factor family. A subfamily.


FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D- lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. SIMILARITY: Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily.


FUNCTION: Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules (By similarity). SIMILARITY: Belongs to the eukaryotic RecA-like protein family.


FUNCTION: Immunity protein that plays a role in preventing early activation of toxin Tse6.


FUNCTION: Probable helicase involved in DNA repair and perhaps also replication. SIMILARITY: Belongs to the helicase family. DinG subfamily.


FUNCTION: Extracellular aminopeptidase that releases a wide variety of amino acids from natural peptides and contributes to pathogenicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M28 family. M28A subfamily.


FUNCTION: DNA-binding protein that regulates the transcription of several genes and is involved in heart development and limb pattern formation. Binds to the core DNA motif of NPPA promoter. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the cytoplasm and the nucleus. Acetylation at Lys-339 promotes nuclear retention.


FUNCTION: Exports L-alanine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AlaE exporter family.


FUNCTION: Zinc transporter that may mediate zinc uptake from the rhizosphere. May also transport other divalent cations. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.


FUNCTION: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the WD repeat ELP2 family.


FUNCTION: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H3 family.


FUNCTION: Glucosyltransferase involved in the biosynthesis of the non- bilayer-prone membrane lipid alpha-monoglucosyldiacylglycerol. This is a major component for maintaining a certain anionic lipid surface charge density, for balancing the bilayer to non-bilayer phase equilibria and for keeping a constant lipid bilayer spontaneous curvature (curvature packing stress). Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D- glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor and DAG is the preferred substrate. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=The enzyme binds the membrane surface via electrostatic association with anionic lipids and is accompanied by hydrophobic interactions and by a conformational change induced by nonbilayer-prone lipids. The enzyme is supposed to be located on the cytosolic side of the membrane. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.


SIMILARITY: Belongs to the glycosyltransferase 2 family.


FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting nfe2l2/nrf2 for ubiquitination (PubMed:18057000). Keap1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of nfe2l2/nrf2, a transcription factor regulating expression of many cytoprotective genes (PubMed:18057000). In response to oxidative stress, different electrophile metabolites trigger non- enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting nfe2l2/nrf2 nuclear accumulation and expression of phase II detoxifying enzymes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly cytoplasmic. SIMILARITY: Belongs to the KEAP1 family.


FUNCTION: Part of the ABC transporter complex TauABC involved in taurine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Taurine importer (TC 3.A.1.17.1) family.


SIMILARITY: Belongs to the UPF0538 family.


FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Enriched in the cortical ER. Concentrated in punctae along the ER tubules. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.


FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol (PubMed:25732826). Displays N-terminal acetyltransferase activity towards a range of N- terminal sequences including those starting with Met-Lys, Met-Val, Met- Ala and Met-Met (PubMed:21750686, PubMed:25732826, PubMed:27550639, PubMed:27320834). Required for normal chromosomal segregation during anaphase (PubMed:21750686). May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences (PubMed:21981917). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Note=Probably forms an intramembrane hairpin-like structure in the membrane. SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily.


FUNCTION: Catalyzes the efflux of phospholipids such as sphingomyelin, cholesterol and its oxygenated derivatives like 7beta- hydroxycholesterol and this transport is coupled to hydrolysis of ATP (PubMed:14668945). The lipid efflux is ALB-dependent. Is an active component of the macrophage lipid export complex. Could also be involved in intracellular lipid transport processes. The role in cellular lipid homeostasis may not be limited to macrophages. Prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cell membrane Note=Predominantly localized in the intracellular compartments mainly associated with the endoplasmic reticulum (ER) and Golgi membranes. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.


FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. In vitro, it can use both NADH and ADP-ribose as substrates; however the relevance of such substrates in vivo is unclear. SIMILARITY: Belongs to the Nudix hydrolase family.


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


FUNCTION: May regulate NF-kappa-B transcription factor activity. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the myotrophin family.


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


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aculenes, a unique type of norsesquiterpenes that contain a nordaucane skeleton linked to an L- proline moiety and are of mixed biosynthetic origin (PubMed:31618514). The pathway begins with the synthesis of dauca-4,7-diene by the terpene cyclase aneC using farnesyl pyrophosphate (FPP) as substrate (PubMed:31618514). The cytochrome P450 monooxygenase aneF then performs the initial oxidation at C-12 of dauca-4,7-diene to yield asperaculane D (PubMed:31618514). Asperaculane D is substrate of the cytochrome P450 monooxygenase aneD for C-10 hydroxylation to yield asperaculane E (PubMed:31618514). The cytochrome P450 monooxygenase aneG then converts asperaculane E into aculene D via C-2 oxidation (PubMed:31618514). The monomodular nonribosomal peptide synthtase aneB adenylates L-proline and the thiohydrolase aneE transfers this activated L-proline derivative to aculenes D and C to produce respectively aculenes B and A (PubMed:31618514). The dioxygenase aneA converts aculene D into aculene C, and aculene B into aculene A by introducing the 5,6-alkene moiety (PubMed:31618514). Asperculanes A, B, C and F, as well as 14-prolyl asperculane C, might be shunt products of the pathway (PubMed:31618514). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs. Does not play a role in replication-dependent histone mRNA degradation. Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2 subfamily.


FUNCTION: Activates macrophages and polarizes them into M1-like macrophages through the activation of the MAPK and NF-kappaB signaling pathway. Upon activation, up-regulates the expression of CD80, CD86, CD69 and MHC II on macrophages, and induces the release of pro- inflammatory cytokines such as TNF, IL1B, IL6, CCL2 and nitric oxide (By similarity). May play a role in inhibition of proliferation and migration (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TMEM106 family.


FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP). SIMILARITY: Belongs to the MoaC family.


FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.


FUNCTION: May function as protective capping of the single-stranded telomeric overhang. May also participate in telomere length regulation during DNA replication. Binds specifically to the T4G4-containing extension on the 3'strand and protects this region of the telomere from nuclease digestion and chemical modification. SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. SIMILARITY: Belongs to the telombin family.


FUNCTION: Acts as a protein folding chaperone for elongation factor 1- alpha. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the nucleus after nutrient stimulation. SIMILARITY: Belongs to the ZPR1 family.


FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=Part of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family.


FUNCTION: Is able to cleave peptidoglycan and affects clumping and separation of bacterial cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the transglycosylase family. SceD subfamily.


FUNCTION: This enzyme catalyzes the endohydrolysis of 1,4-beta- glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.


FUNCTION: ADP-ribosylhydrolase that preferentially hydrolyzes the scissile alpha-O-linkage attached to the anomeric C1'' position of ADP- ribose and acts on different substrates, such as proteins ADP- ribosylated on serine and threonine, free poly(ADP-ribose) and O- acetyl-ADP-D-ribose. Specifically acts as a serine mono-ADP- ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to serine residues on proteins, thereby playing a key role in DNA damage response. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Does not hydrolyze ADP-ribosyl-arginine, -cysteine, -diphthamide, or -asparagine bonds. Also able to degrade protein free poly(ADP-ribose), which is synthesized in response to DNA damage: free poly(ADP-ribose) acts as a potent cell death signal and its degradation by ADPRHL2 protects cells from poly(ADP-ribose)-dependent cell death, a process named parthanatos (By similarity). Also hydrolyzes free poly(ADP- ribose) in mitochondria. Specifically digests O-acetyl-ADP-D-ribose, a product of deacetylation reactions catalyzed by sirtuins. Specifically degrades 1''-O-acetyl-ADP-D-ribose isomer, rather than 2''-O-acetyl- ADP-D-ribose or 3''-O-acetyl-ADP-D-ribose isomers. SUBCELLULAR LOCATION: Nucleus Cytoplasm Chromosome Mitochondrion matrix Note=Recruited to DNA lesion regions following DNA damage; ADP-D-ribose-recognition is required for recruitment to DNA damage sites. SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.


FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 5DNU family.


FUNCTION: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Binds AI-2 and delivers it to the LsrC and LsrD permeases (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.


SIMILARITY: Belongs to the herpesviridae U4 family.


FUNCTION: Plays a role in the organization of the actin cytoskeleton. May function as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. May decrease the metastatic potential of tumors. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection. SIMILARITY: Belongs to the actin family. ARP3 subfamily.


FUNCTION: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6- sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6- sulfate-(1->3)-beta-D-galactose. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 16 family.


FUNCTION: Plays a central regulatory role in DNA repair and protection pathways in response to radiation stress (PubMed:12804570, PubMed:22051194). Acts as a site-specific metalloprotease that cleaves and inactivates the repressor protein DdrO, resulting in induced expression of genes required for DNA repair and cell survival after exposure to radiation (By similarity). Regulates the expression of dozens of proteins from different pathways, including the important DNA repair proteins RecA and PprA (PubMed:12399492, PubMed:12804570, PubMed:22051194). Binds to the promoters of recA and pprA (PubMed:22051194).


FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of aspulvinones (PubMed:29305695, PubMed:23841722, PubMed:28791090). The nonribosomal peptide synthetase apvA is responsible for the production of aspulvinone E, the core structure of aspulvinones (PubMed:29305695, PubMed:23841722, PubMed:28791090). ApvA first activates 4-hydroxyphenylpyruvate (HPPA) through its A domain to AMP-HPPA (Probable). The HPPA unit is then loaded to the T domain and eventually transferred to the TE domain (Probable). Upon loading of another HPPA unit to the T domain, the TE domain promotes the enolate formation on the unit attached (Probable). The next step involves head to tail Claisen condensation, followed by the keto-enol tautermerization and a nucleophilic attack on the carbonyl carbon to yield the furanone partial structure (Probable). A spontaneous oxidation at the beta-carbon of the thioester might occur in aerobic condition (Probable). The TE domain then catalyzes the hydrolysis of the thioester, followed by spontaneous decarboxylation, dehydroxylation and keto-enol tautermerization to give the aspulvinone core (Probable). Aspulvinone E is highly unstable and converted to isoaspulvinone E in the presence of light (PubMed:29305695). The structural diversity of the aspulvinones suggests that other tailoring enzymes are involved and have still to be identified (Probable). SIMILARITY: Belongs to the NRP synthetase family.


FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases Cdk1 and Cdk2, and is essential for their biological function. SIMILARITY: Belongs to the CKS family.


FUNCTION: Member of the two-component regulatory system SaeR/SaeS involved in the regulation of staphylococcal virulence factors in a strain-dependent fashion. Probably functions as a membrane-associated protein kinase that upon sensing the appropriate signal, autophosphorylates and in turn activates the cytosolic response regulator SaeR. SaeR/SaeS activates the expression of exoproteins involved in adhesion and invasion of host cells, including hemolysins (hla, hlb, hlgC), coa, DNase, spa and cell wall-associated proteins (emp, eap, fnbA, fnbB, efb). Represses the expression of type 5 capsular polysaccharide (cap operon). Also modulates the expression of several other genes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


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


FUNCTION: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner (PubMed:7544779, PubMed:7836368, PubMed:9654122). Has no activity towards all-trans retinal (PubMed:9654122). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE) (By similarity). Also recognizes steroids (androsterone, androstanediol) as its substrates (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein; Lumenal side Microsome membrane. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.


FUNCTION: This protein is probably a component of a manganese permease, a binding protein-dependent, ATP-driven transport system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.


FUNCTION: Plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Its association with piP-bodies suggests a participation in the secondary piRNAs metabolic process. Required for the localization of germ-cell factors to the meiotic nuage (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Specifically localizes to piP-bodies, a subset of the nuage which contains secondary piRNAs (By similarity). SIMILARITY: Belongs to the maelstrom family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the complex I 30 kDa subunit family.


FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 2 family.


FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta- 3 is involved in the regulation of lipolysis and thermogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB3 sub-subfamily.


FUNCTION: Essential for n-decane utilization. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.


FUNCTION: Transcription factor that binds 5'-AACGG-3' motifs in gene promoters (By similarity). Required for proper circadian rhythm (PubMed:18426557). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Involved in rRNA-processing and ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP23/FCF1 family. UTP23 subfamily.


SIMILARITY: Belongs to the ODF3 family.


SIMILARITY: Belongs to the UPF0248 family.


FUNCTION: Prevents homeodomain proteins (e.g. STM) association to plasmodesmata and, consequently, cell-to-cell transport. Binds to RNA. Alters STM RNA binding capacity (PubMed:17965274). Regulates cytoskeleton (e.g. actin) organization that determinates cell shape (PubMed:8893552, PubMed:19074626). Regulates stomata patterning and drought tolerance (PubMed:19074626). Involved in restricting tobamovirus (e.g. oilseed rape mosaic virus) infectivity, probably by interfering with cell-to-cell virus movement (PubMed:19074626). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Microtubule-associated and stabilizer (PubMed:17965274, PubMed:19074626). Localized in cytosolic punctae when associated with STM (PubMed:17965274). SIMILARITY: Belongs to the microtubule binding protein 2C family.


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


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


FUNCTION: Likely catalyzes the dephosphorylation of O-phospho-L-serine into L-serine. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.


SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.


FUNCTION: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria (PubMed:25313960, PubMed:31983639). Constitutes a pore-forming and calcium-conducting subunit (By similarity). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways (By similarity). Required for rapid mitochondrial calcium uptake and mitochondrial reactive oxygen species (mtROS) production after wounding (PubMed:25313960). In addition, together with mitochondrial calcium regulator micu-1, required for mitochondrial calcium uptake following axon injury in PLM touch receptor neurons (PubMed:31983639). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MCU (TC 1.A.77) family.


FUNCTION: Involved in endocytic trafficking by stabilizing organelles of the endocytic pathway. Probably acts as a cytoskeletal linker protein required to tether endosome vesicles to the cytoskeleton. Involved in modulation of endocytosis at stages required for down- regulation of membrane proteins that control synapse size. Not involved in synaptic vesicle recycling. Required in R7 cells for boss endocytosis into multivesicular bodies (MVBs). Has a role in regulating adult longevity. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Endosome Synapse Note=Enriched at neuromuscular synapses, in both presynaptic and postsynaptic regions. SIMILARITY: Belongs to the hook family.


FUNCTION: Forms a complex at the inner spore membrane which acts as a receptor for L-alanine, thus is involved in the stimulation of germination in response to alanine. Can stimulate germination in the absence of GerD and GerK gene products (fructose and glucose receptors, respectively), but the response is improved in their presence. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GerABKA family.


FUNCTION: Phosphorylates the sporulation-regulatory protein Spo0A a transcription factor that also controls biofilm formation (Probable). Requires FloT and FloA for localization to DRMs and for activity (PubMed:20713508). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Membrane raft; Multi-pass membrane protein Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic membrane rafts; these rafts include proteins involved in signaling, molecule trafficking and protein secretion. Lost from DRM in the absence of farnesyl diphosphate phosphatase YisP or when cells are treated with YisP inhibitor zaragozic acid. Colocalizes with FloT in DRMs (PubMed:20713508, PubMed:26297017). Another study shows KinC foci are membrane assemblies of 85-110 nm, but found no evidence of colocalization of these foci with FloA or FloT (PubMed:27362352).


FUNCTION: May subvert the host innate immune response by interacting with host IL1B and interfering with its function. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the asfivirus L83L family.


FUNCTION: Transcription factor of the NAC family. May be associated with anther development and pollen production (Probable). Required for normal seed development and morphology (PubMed:18849494). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Probable transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Probably acts by participating in large multiprotein complexes that represses transcription of GA-inducible genes. Upon GA application, it is degraded by the proteasome, allowing the GA signaling pathway (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GRAS family. DELLA subfamily.


FUNCTION: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain. Potently activated by enkephalins (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily.


FUNCTION: Putative tail fiber protein. SUBCELLULAR LOCATION: Virion. SIMILARITY: To phage P22 head-binding domain.


FUNCTION: May play a role in signal transduction pathways that involve calcium as a second messenger. SUBCELLULAR LOCATION: Membrane; Lipid-anchor. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily.


FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. FUNCTION: Bifunctional enzyme that catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L- lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives, and the FMNH2- dependent reduction of dehydro-F420-0 to form F420-0. SIMILARITY: In the N-terminal section; belongs to the CofE family. SIMILARITY: In the N-terminal section; belongs to the CofE family.


FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the UbiD family.


FUNCTION: Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import. Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. May be involved in nuclear localization of XPA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the GPN-loop GTPase family.


FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen oxidase family. Coproporphyrinogen III oxidase subfamily.


FUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes (PubMed:17998332, PubMed:18838538, PubMed:20516061). Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (PubMed:17998332, PubMed:18838538). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33913806, PubMed:33767452). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452). FUNCTION: Regulatory component of the SET1 complex implicated in the tethering of this complex to transcriptional start sites of active genes (By similarity). Facilitates histone H3 'Lys-4' methylation (H3K4me) via recruitment of the SETD1A or SETD1B to the 'Ser-5' phosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A) (By similarity). Component of PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (By similarity). Together with ZC3H4, but independently of the SET1 complex, part of a transcription termination checkpoint that promotes transcription termination of long non-coding RNAs (lncRNAs) (PubMed:33767452). The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs and promotes transcription termination of lncRNAs and their subsequent degradation by the exosome (PubMed:33767452). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associates with chromatin (By similarity). Recruited at sites of high RNA polymerase II occupancy (PubMed:33767452). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associates with chromatin (PubMed:20516061). Recruited at sites of high RNA polymerase II occupancy (By similarity). SIMILARITY: Belongs to the WD repeat SWD2 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MIT-like AcTx family.


FUNCTION: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. CcmA exporter (TC 3.A.1.107) family.


FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence- specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3' (By similarity). SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.


FUNCTION: This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uL5 family.


FUNCTION: Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria. SUBCELLULAR LOCATION: Cytoplasm, cytosol Mitochondrion Nucleus Cytoplasm, cytoskeleton Cell projection, axon Note=Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor (PubMed:21730050). Colocalized with MAPT/TAU in the distal part of the primary cortical neurons (By similarity).


FUNCTION: May have a role in cell wall processes (PubMed:26177502). Does not exhibit cutinase activity (PubMed:19225166). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Secreted, cell wall. SIMILARITY: Belongs to the cutinase family.


SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the dynein light chain family.


FUNCTION: May play a role in transgenerational epigenetic inheritance.


FUNCTION: Protease required for deconjugation of smo-1 conjugates from target proteins which is necessary for cell cycle progression (PubMed:25475837) (Probable). Required for respiration and the maintenance of normal mitochondrial homeostasis (PubMed:25187565). In response to mitochondrial stress, required for the removal of smo-1 conjugates from the transcription factor dve-1, which promotes the translocation of dve-1 from the cytosol to the nucleus to initiate the mitochondrial unfolded protein response (PubMed:30642431). Furthermore, removes the smo-1 conjugates from the transcription factor atfs-1 to promote its stability and activate the mitochondrial unfolded protein response (PubMed:30642431). Also plays a role in promoting mitochondrial unfolded protein response-mediated innate immunity following infection with P.aeruginosa (PubMed:30642431). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm Mitochondrion matrix Note=Localizes around the metaphase plate and the pericentriolar region and in the surroundings of the central spindle (PubMed:25475837). Translocates from cytoplasm to mitochondrion at late developmental stages (PubMed:25187565). SIMILARITY: Belongs to the peptidase C48 family.


FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (By similarity). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation (By similarity). Fc-binding subunit that associates with FCER1G adapter to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapter with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.


FUNCTION: Required for respiratory activity and maintenance and expression of the mitochondrial genome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRG8 family.


FUNCTION: Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3- diphosphoglycerate by NADPH (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.


FUNCTION: Probable protein tyrosine phosphatase. Has phosphatase activity with synthetic substrates (PubMed:15252030, PubMed:29106959). Has a phosphatase activity-independent regulatory role in MAP3K5/ASK1- mediated apoptosis, preventing MAP3K5/ASK1 inhibition by AKT1. Shows no phosphatase activity on MAPK1/ERK2, MAPK8/JNK, MAPK14/p38 and MAP3K5/ASK1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.


FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (By similarity). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE- conjugated forms of ATG8 proteins during macroautophagy. Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity. In contrast to other members of the family, weakly or not involved in phagophore growth during mitophagy (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C54 family.


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; Peripheral membrane protein; Matrix side Note=The interaction with BCAP31 mediates mitochondria localization. SIMILARITY: Belongs to the complex I NDUFS4 subunit family.


SUBCELLULAR LOCATION: Cytoplasm Note=Colocalizes with vimentin-type intermediate filaments.


FUNCTION: Lectin specific for high mannose N-glycans, recognizes the branched moiety of these glycans. Does not recognize other types of N- glycans or monosaccharides. SIMILARITY: Belongs to the bacterial lectin family.


FUNCTION: RNA-binding protein implicated in numerous RNA metabolic processes. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. Mitochondrial intermembrane factor with RNA-processing exoribonulease activity. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. Involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules (By similarity). Required for correct processing and polyadenylation of mitochondrial mRNAs. Plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Plays a role in mitochondrial morphogenesis and respiration; regulates the expression of the electron transport chain (ETC) components at the mRNA and protein levels. In the cytoplasm, shows a 3'-to-5' exoribonuclease mediating mRNA degradation activity; degrades c-myc mRNA upon treatment with IFNB1/IFN-beta, resulting in a growth arrest in melanoma cells. Regulates the stability of specific mature miRNAs in melanoma cells; specifically and selectively degrades miR-221, preferentially. Also plays a role in RNA cell surveillance by cleaning up oxidized RNAs. Binds to the RNA subunit of ribonuclease P, MRP RNA and miR-221 microRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion matrix Mitochondrion intermembrane space; Peripheral membrane protein. SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase family.


FUNCTION: Involved in ammonium transport. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase D subunit family.


FUNCTION: In vitro, inhibits proliferation of the mice ovarian cancer cells ID8. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family.


FUNCTION: Autophagic substrate degraded in the vacuole by non-selective autophagy. Requires ATG8 protein expression to be recognized as an autophagic substrate (PubMed:21606687). Acts probably as a receptor for autophagosomal degradation of ubiquitinated proteins. Targets ubiquitinated protein aggregates derived from denatured or damaged non- native proteins generated under stress conditions (PubMed:23341779). Functions additively with the E3 ubiquitin-protein ligase CHIP for autophagosomal degradation of proteotoxic aggregates formed under stress conditions (PubMed:24497840). SUBCELLULAR LOCATION: Cytoplasm Vacuole Note=Forms large punctated cytoplasmic structures. Recruited to the central vacuole by non-selective autophagy.


FUNCTION: Catalyzes the interconvertion of dTDP-6-deoxy-L-talose and dTDP-L-rhamnose. The equilibrium is strongly toward dTDP-L-rhamnose. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family.


FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.


SIMILARITY: Belongs to the SCO1/2 family.


FUNCTION: Antimicrobial activity against the Gram-positive bacterium S.aureus. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily.


FUNCTION: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase delta chain family.


FUNCTION: Component of the toluene-4-monooxygenase multicomponent enzyme system which catalyzes the O2- and NADH-dependent hydroxylation of toluene to form p-cresol (PubMed:1885512, PubMed:15240250, PubMed:2019563, PubMed:19290655, PubMed:19705873). Also able to convert benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by successive hydroxylations (PubMed:15240250). SIMILARITY: Belongs to the TmoB/XamoB family.


SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. SIMILARITY: Belongs to the RMDN family.


FUNCTION: Catalyzes the interconversion of L-alpha-lysine and L-beta- lysine. Is involved in the biosynthesis pathway of N6-acetyl-beta- lysine, a compatible solute produced by methanogenic archaea that helps cells to cope with salt stress. SIMILARITY: Belongs to the radical SAM superfamily. KamA family.


FUNCTION: Allophycocyanin is a photosynthetic bile pigment-protein complex with maximum absorption at approximately 650 nanometers. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family.


FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.


FUNCTION: RNA chaperone with significant RNA binding, RNA strand exchange and RNA duplexing activities. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ProQ family.


FUNCTION: Produces a single-strand nick in a specific site of the plasmid, and this nick results in single-strand replication by rolling circle mechanism. SIMILARITY: Belongs to the Gram-positive plasmids replication protein type 1 family.


FUNCTION: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the cytochrome c family.


FUNCTION: ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA subfamily.


FUNCTION: Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide. SUBCELLULAR LOCATION: Mitochondrion.


FUNCTION: Plays an essential role in the production of budded virions (BVs) as well as in the envelopment of occluded derived virions (ODVs). SUBCELLULAR LOCATION: Host nucleus Host cytoplasm. SIMILARITY: Belongs to the baculoviridae p48 family.


FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation (Probable). May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton (Probable). ATG8CL-mediated selective autophagy contributes to defense against the fungal pathogen Phytophtora infestans (PubMed:26765567, PubMed:29932422). SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Lipid- anchor Vacuole membrane; Lipid-anchor Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the ATG8 family.


FUNCTION: MYB-type transcription factor involved in epidermal cell fate specification. Acts as a negative regulator of trichome development, including endoreplication, by mediating lateral inhibition. Promotes the formation of hair developing cells in H position in root epidermis, probably by inhibiting non-hair cell formation. May have pleiotropic effects on flowering development and epidermal cell size through the regulation of endoreduplication. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 17 family.


FUNCTION: Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the small GTPase superfamily. Ras family. KappaB-Ras subfamily.


FUNCTION: Probable toxin that belongs to the MSDIN-like toxin family responsible for a large number of food poisoning cases and deaths (PubMed:24050899). SIMILARITY: Belongs to the MSDIN fungal toxin family.


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 spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The Cas4 region acts as a ssDNA exonuclease, while the Cas1 region acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated exonuclease Cas4 family. SIMILARITY: In the C-terminal section; belongs to the CRISPR-associated endonuclease Cas1 family.


SIMILARITY: Belongs to the UPF0482 family.


FUNCTION: Contributes to the transparency and refractive index of the lens. Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions. Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. SIMILARITY: Belongs to the small heat shock protein (HSP20) 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 I subfamily. D49 sub-subfamily.


FUNCTION: Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT3 and more rarely with PMT2 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 39 family.


FUNCTION: Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


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


FUNCTION: Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP) (By similarity). Promotes apoptosis. SUBCELLULAR LOCATION: Mitochondrion Note=Released into the cytosol when cells undergo apoptosis.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids without apparent head group selectivity (PubMed:12522102, PubMed:18801741, PubMed:15863501, PubMed:28947740). Contributes to phospholipid remodeling of low-density lipoprotein (LDL) and high-density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (PubMed:18801741). May act in an autocrine and paracrine manner (PubMed:23624557). Secreted by immature mast cells, acts on nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2 (PGD2), which in turn promotes mast cell maturation and degranulation via PTGDR (PubMed:23624557). Secreted by epididymal epithelium, acts on immature sperm cells within the duct, modulating the degree of unsaturation of the fatty acyl components of phosphatidylcholines required for acrosome assembly and sperm cell motility. Facilitates the replacement of fatty acyl chains in phosphatidylcholines in sperm membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6 PUFAs to generate oxygenated lipid mediators in the male reproductive tract (By similarity). At pericentrosomal preciliary compartment, negatively regulates ciliogenesis likely by regulating endocytotic recycling of ciliary membrane protein (PubMed:20393563). Coupled to cyclooxygenase pathway provides arachidonate to generate prostaglandin E2 (PGE2), a potent immunomodulatory lipid in inflammation and tumorigenesis (PubMed:12522102, PubMed:15863501). At colonic epithelial barrier, preferentially hydrolyzes phospholipids having arachidonate and docosahexaenoate at sn-2 position, contributing to the generation of oxygenated metabolites involved in colonic stem cell homeostasis (PubMed:28947740). Releases C16:0 and C18:0 lysophosphatidylcholine subclasses from neuron plasma membranes and promotes neurite outgrowth and neuron survival (PubMed:17868035). SUBCELLULAR LOCATION: Secreted Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Recycling endosome Note=Localized at pericentrosomal preciliary compartment. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauB domain of TFIIIC that binds boxB DNA promoter sites of tRNA and similar genes. Cooperates with TFC3 in DNA binding. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Forms short fibers at the surface of the viral capsid. SUBCELLULAR LOCATION: Virion Note=Present in 75 copies in the virion.


FUNCTION: Involved in pre-mRNA splicing as a component of the splicing factor SF3A complex that contributes to the assembly of the 17S U2 snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' complex (PubMed:10882114, PubMed:11533230). Involved in pre-mRNA splicing as a component of pre- catalytic spliceosome 'B' complexes (PubMed:29360106, PubMed:30315277). SUBCELLULAR LOCATION: Nucleus Nucleus speckle.


FUNCTION: Endonuclease which induces a single-strand cut at or near ori. May act by forming a covalent link to the 5'side of the nick. SIMILARITY: Belongs to the phage GPA family.


FUNCTION: Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the small GTPase superfamily. Rho family.


SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the peptidase M16 family.


FUNCTION: Can suppress the synthetic lethality of the hal3 sit4 double mutation when overexpressed, suggesting that it is involved in the G1-S transition. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: To yeast MFL3.


FUNCTION: This highly disulfide-bonded protein is a potent inhibitor of factor Xa. May have therapeutic utility as an anticoagulant. Also exhibits a strong metastatic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family.


FUNCTION: Binds 23S rRNA. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the universal ribosomal protein uL6 family.


FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF- 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF- 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.


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


FUNCTION: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation (By similarity). SIMILARITY: Belongs to the prokaryotic ubiquitin-like protein family.


FUNCTION: Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its not yet determined substrates. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Gustatory receptor (GR) family. Gr2a subfamily.


FUNCTION: Non-catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. May play a role in normal cell-cycle progression. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MDM20/NAA25 family.


FUNCTION: May negatively regulate cell cycle progression. May act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F-dependent transcription. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the CCNDBP1 family.


FUNCTION: Component of the cytoplasmic filaments that run the length of the organism just underneath the cytoplasmic membrane. SUBCELLULAR LOCATION: Cytoplasm. Note=An array of 4 to 6 filaments lie in close apposition to the inner membrane and are always localized directly underneath the corresponding group of periplasmic flagella.


FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). SIMILARITY: Belongs to the V-ATPase F subunit family.


FUNCTION: Inhibits trypsin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I7 (squash-type serine protease inhibitor) family.


FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFB5 family.


FUNCTION: May act as a regulator of cilium basal body docking and positioning in mono- and multiciliated cells. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. SIMILARITY: Belongs to the Flattop family.


FUNCTION: Probable transporter. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


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. SIMILARITY: Belongs to the type II topoisomerase family. ParE type 1 subfamily.


FUNCTION: One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS17 family.


FUNCTION: May cause loosening of the cell walls. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the expansin family. Expansin B subfamily.


FUNCTION: Terpene synthase that catalyzes the conversion of (2E,6E)- farnesyl diphosphate (FPP) into sesquiterpenes which are important for fungi-environment interactions (PubMed:31239482). Produces a mixture consisting of 8 sesquiterpenes including corvol ethers A and B, as well as traces of epizonarene, gamma-cadinene, delta-cadinene, alpha- cadinene, alpha-cadinol, and an unidentified sesquiterpene (PubMed:31239482). The major product is corvol ether B (PubMed:31239482). SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell projection, dendrite Note=Localizes in mRNA granules in dentrites.


FUNCTION: May play a role in transcription or DNA repair. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the enhancer of polycomb family.


SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the class A bacterial acid phosphatase family.


FUNCTION: Catalyzes the opening of the heme ring with the release of iron. Key enzyme in the synthesis of the chromophoric part of the photosynthetic antennae (By similarity). Upon overexpression in E.coli with PCB:ferredoxin oxidoreductase, CpeS and either CpcB or PecB permits synthesis of phycocyanin-coupled CpcB or PecB. SIMILARITY: Belongs to the heme oxygenase family.


FUNCTION: Cardiolipin hydrolase present at the mitochondrial outer membrane required for piRNA metabolic process. Acts by catalyzing the hydrolysis of cardiolipin (diphosphatidylglycerol) to form phosphatidate (phosphatidic acid or PA) at the mitochondrial outer membrane surface, promoting the piRNA metabolic process. Plays a key role in primary biogenesis of piRNAs and is required during oogenesis to repress transposable elements and prevent their mobilization. piRNAs mediate the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Involved in trans-silencing effect (TSE), a homology-dependent repression mechanism by which a P-transgene inserted in subtelomeric heterochromatin via its role in piRNA biogenesis. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Note=Was initially reported to localize to the meiotic nuage, also named P granule (PubMed:17543859). However, it was later shown that the EGFP tag at N-terminus used in initial experiments interfered with mitochondrial localization (PubMed:21397848, PubMed:20966047). SIMILARITY: Belongs to the phospholipase D family. MitoPLD/Zucchini subfamily.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids (PubMed:10681567, PubMed:11922621, PubMed:28883454). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), releasing various unsaturated fatty acids including oleoate, linoleoate, arachidonate, docosahexaenoate and lysophosphatidylethanolamines in preference to lysophosphatidylcholines (PubMed:10681567, PubMed:28883454). In response to high-fat diet, hydrolyzes minor lipoprotein phospholipids including phosphatidylserines, phosphatidylinositols and phosphatidylglycerols, altering lipoprotein composition and fat storage in adipose tissue and liver (By similarity). May act in an autocrine and paracrine manner (PubMed:11922621). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of phosphatidylglycerols and phosphatidylethanolamines, which are major components of membrane phospholipids in bacteria (PubMed:11922621). Acts as a hair follicle phospholipase A2. Selectively releases lysophosphatidylethanolamines (LPE) and various unsaturated fatty acids in skin to regulate hair follicle homeostasis (By similarity). May regulate the inflammatory response by releasing arachidonate, a precursor of prostaglandins and leukotrienes (PubMed:11922621). Upon allergen exposure, may participate in allergic inflammatory response by enhancing leukotriene C4 synthesis and degranulation in mast cells (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Through binding to heparan sulfate proteoglycan, may be localized to cytoplasmic compartments enriched in anionic phospholipids. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complexes, to modulate their activities. Recognizes the host NF-kappa-B regulator BTRC through the presence of a DSGXS motif in the C-terminal substrate recognition domain. SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton. SIMILARITY: Belongs to the rotavirus NSP1 family.


FUNCTION: May play a role in chromosome segregation through establishment of sister chromatid cohesion. SIMILARITY: Belongs to the MIP18 family.


FUNCTION: Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1. SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the COG4 family.


FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.


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


FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase delta chain family.


FUNCTION: Transcription activation. Regulates the delayed-early 110 kDa promoter. SIMILARITY: Belongs to the herpesviridae TAF50 family.


FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Acts as a functional inhibitor of gH and maintains gH in an inhibited form. Upon binding to host integrins, gL dissociates from gH leading to activation of the viral fusion glycoproteins gB and gH (By similarity). In human cytomegalovirus, forms two distincts complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA. The gH-gL- UL128-UL130-UL131A pentamer is essential for viral entry in epithelial, endothelial and myeloid cells via interaction with host NRP2 (By similarity). SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein; Extracellular side Host cell membrane; Peripheral membrane protein; Extracellular side Host Golgi apparatus, host trans- Golgi network Note=gL associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the host trans-Golgi where secondary envelopment occurs. SIMILARITY: Belongs to the herpesviridae glycoprotein L family.


FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of mRNAs. SIMILARITY: Belongs to the pseudouridine synthase TruD family.


FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the uricase family.


FUNCTION: Methylthiotransferase that catalyzes the conversion of N6- (dimethylallyl)adenosine (i(6)A) to 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 (adjacent to the 3'-end of the anticodon) of four mitochondrial DNA-encoded tRNAs (Ser(UCN), Phe, Tyr and Trp) (By similarity). Essential for efficient and highly accurate protein translation by the ribosome (By similarity). Specifically inhibits CDK5 activation by CDK5R1 (By similarity). Essential for efficient mitochondrial protein synthesis and respiratory chain (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily.


SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the OSBP family.