FUNCTION: Antibacterial protein. Putative acid-stable proteinase inhibitor (By similarity). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Contributes to activation of immediate-early gene expression. SUBCELLULAR LOCATION: Virion Host nucleus Host cytoplasm Note=Expressed exclusively within the host nucleus in early times of infection and then present in both nucleus and cytoplasm at 72 hours post infection. SIMILARITY: Belongs to the herpesviridae US22 family.


FUNCTION: May be involved in the biogenesis of curli organelles. FUNCTION: May be involved in the biogenesis of curli organelles.


FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth. FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the KRR1 family. SIMILARITY: Belongs to the KRR1 family.


FUNCTION: Required for formation of the 2-thio group of the 5- methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs. SUBCELLULAR LOCATION: Mitochondrion Cytoplasm.


FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity). SIMILARITY: Belongs to the V-ATPase E subunit family.


FUNCTION: This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family.


SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins (By similarity). Together with ubc-18, required for the ubiquitination of membranous organelles, and the removal of paternal mitochondria from early embryos (PubMed:31153831). SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scolopendra neurotoxin 10 family.


FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of 15-deoxyoxalicine B (PubMed:30090271). The first step of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by the nicotinic acid-CoA ligase olcI (PubMed:30090271). Nicotinyl-CoA is then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the polyprenyl transferase olcH to yield geranylgeranyl-HPPO (PubMed:30090271). Geranylgeranyl pyrophosphate is provided by the cluster-specific geranylgeranyl pyrophosphate synthase olcC (PubMed:30090271). The FAD-dependent monooxygenase olcE catalyzes the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD catalyzes the cyclization of the terpenoid component, resulting in the formation of the tricyclic terpene moiety seen in predecaturin E (PubMed:30090271). The cytochrome P450 monooxygenase then catalyzes the allylic oxidation of predecaturin E, which is followed by spirocylization with concomitant loss of one molecule of water to form decaturin E (PubMed:30090271). Decaturin E is the substrate of the cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29 position to form decaturin F (PubMed:30090271). The short-chain dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F to generate the 29-hydroxyl-27- one intermediate, and subsequent hemiacetal formation probably leads to the formation of decaturin C (Probable). The dioxygenase olcK may be a peroxisomal enzyme that catalyzes the hydroxylation of decaturin C into decaturin A once decaturin C is shuttled into the peroxisome by the MFS transporter olcL (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes the oxidative rearrangement to yield 15-deoxyoxalicine B (PubMed:30090271). In the absence of olcJ, decaturin E may be shunted to a pathway in which it is oxidized to a ketone, possibly by olcF, to form decaturin D, which undergoes further allylic oxidation to yield decaturin G (PubMed:30090271). Moreover, in the absence of oclK or oclL, oclB can convert decaturin C into 15-deoxyoxalicine A (PubMed:30090271). SIMILARITY: Belongs to the FPP/GGPP synthase family.


FUNCTION: Putative surfactant protein. SUBCELLULAR LOCATION: Secreted Cytoplasmic vesicle, secretory vesicle Golgi apparatus.


FUNCTION: Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. DltA subfamily.


FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein linkage region (GlcUAbeta1-3Galbeta1-3Galbeta1-4Xylbeta1-O-Ser) of core proteins, which is formed by the stepwise addition of monosaccharide residues by the respective specific glycosyltransferases. Xylose 2-O- phosphorylation may influence the catalytic activity of B3GAT3 (GlcAT- I) which completes the precursor tetrasaccharide of GAG-protein linkage regions on which the repeating disaccharide region is synthesized. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the FAM20 family.


FUNCTION: Metalloprotease. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy- D-galactonate. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. GalD subfamily.


FUNCTION: Catalyzes the reduction of free and protein-bound methionine sulfoxide to methionine. SUBCELLULAR LOCATION: Endoplasmic reticulum Note=Not detected in the mitochondrion. SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.


FUNCTION: Putative component of the fimbrium tip. Fimbriae are filamentous appendages on the cell surface that mediate cell adhesion and biofilm formation. SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily. FimA/Mfa1 family.


FUNCTION: Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. Sar1 controls the coat assembly in a stepwise manner. Activated Sar1-GTP binds to membranes first and recruits the sec23/24 complex. These sec23/24-sar1 prebudding intermediates are then collected by the Sec13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to sar1-GDP triggers coat release and recycles COPII subunits (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.


FUNCTION: Receptor for Wnt proteins. Acts in both canonical and non- canonical Wnt pathways. Although different papers report differing Wnt preferences, wnt5a, wnt8b and wnt11 have been proposed as synergists. In the canonical Wnt pathway, acts via beta-catenin to promote the expression of the dorsal genes siamois, twin and nodal3 and to establish the dorsal axis of the embryo and induce dorsal mesoderm formation. In a non-canonical Wnt/planar cell polarity (PCP) pathway, acts with sdc4 and dvl2/dsh to regulate convergent extension cell movements during gastrulation. Triggers phosphorylation of dvl2/dsh and its translocation to the plasma membrane. In a third branch of Wnt signaling, acts in a non-canonical pathway via trimeric G proteins, and independently of dvl2/dsh, to recruit protein kinase C (PKC) to the membrane and thus activate PKC. PKC signaling controls cell sorting and tissue separation during gastrulation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinositol 4,5-bisphosphate (PIP2). Localized in recycling endosomes in other conditions. SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.


FUNCTION: Flavin-dependent enoate reductase that catalyzes the chemo- and stereoslective hydrogenation of electron-poor alkenes. The enzyme is reduced by NADPH, and oxygen, quinones, and alpha,beta- unsaturated aldehydes and ketones can act as electron acceptors to complete catalytic turnover. The physiological oxidant remains elusive. SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family.


FUNCTION: Mitochondrial iron transporter that mediates iron uptake. Probably required for heme synthesis of hemoproteins and Fe-S cluster assembly in non-erythroid cells. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


SIMILARITY: Belongs to the complex I 20 kDa subunit family.


FUNCTION: Catalyzes the N-methylation of nicotinamide using the universal methyl donor S-adenosyl-L-methionine to form N1- methylnicotinamide and S-adenosyl-L-homocysteine, a predominant nicotinamide/vitamin B3 clearance pathway (PubMed:8182091, PubMed:21823666, PubMed:23455543). Plays a central role in regulating cellular methylation potential, by consuming S-adenosyl-L-methionine and limiting its availability for other methyltransferases. Actively mediates genome-wide epigenetic and transcriptional changes through hypomethylation of repressive chromatin marks, such as H3K27me3 (PubMed:26571212, PubMed:23455543, PubMed:31043742). In a developmental context, contributes to low levels of the repressive histone marks that characterize pluripotent embryonic stem cell pre-implantation state (PubMed:26571212). Acts as a metabolic regulator primarily on white adipose tissue energy expenditure as well as hepatic gluconeogenesis and cholesterol biosynthesis. In white adipocytes, regulates polyamine flux by consuming S-adenosyl-L-methionine which provides for propylamine group in polyamine biosynthesis, whereas by consuming nicotinamide controls NAD(+) levels through the salvage pathway (By similarity). Via its product N1-methylnicotinamide regulates protein acetylation in hepatocytes, by repressing the ubiquitination and increasing the stability of SIRT1 deacetylase (By similarity). Can also N-methylate other pyridines structurally related to nicotinamide and play a role in xenobiotic detoxification (PubMed:30044909). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.


FUNCTION: With EpmB is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF- P). Catalyzes the ATP-dependent activation of (R)-beta-lysine produced by EpmB, forming a lysyl-adenylate, from which the beta-lysyl moiety is then transferred to the epsilon-amino group of a conserved specific lysine residue in EF-P. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. EpmA subfamily.


FUNCTION: Structural protein that is specific for occlusion-derived virus (ODV) envelopes but not of budded virus (BV). SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Note=Localized to the envelope region of preoccluded bundles of virions. SIMILARITY: Belongs to the baculoviridae E56 family.


FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of arpp19 and ensa at 'Ser- 67', 2 phosphatase inhibitors that specifically inhibit the ppp2r2d (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.


FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. FUNCTION: Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20713600, PubMed:24290141). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20713600). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538, PubMed:31006537). SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor Endomembrane system; Lipid-anchor Cytoplasm, cytoskeleton Note=LC3-II binds to the autophagic membranes. SUBCELLULAR LOCATION: Endomembrane system; Lipid-anchor Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor Cytoplasmic vesicle, autophagosome Cytoplasm, cytoskeleton Note=LC3-II binds to the autophagic membranes. SUBCELLULAR LOCATION: Endomembrane system; Lipid-anchor Cytoplasmic vesicle, autophagosome membrane; Lipid-anchor Cytoplasmic vesicle, autophagosome Cytoplasm, cytoskeleton Note=LC3-II binds to the autophagic membranes. SIMILARITY: Belongs to the ATG8 family.


FUNCTION: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I- branching enzyme activity by converting linear into branched poly-N- acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 14 family.


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


FUNCTION: Part of an energy-coupled inorganic carbon pump. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabA family.


FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit D family.


SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor Note=Distributed in a discrete, punctate pattern with up to 3 loci per cell over the surface (PubMed:18800056). Does not localize with ClfA (PubMed:18800056). Exchanging the ClfA and SasF signal peptides retargets the mature protein on the cell surface (PubMed:18800056). Anchored to the cell wall by sortase A (Probable).


SIMILARITY: Belongs to the glycosyl hydrolase 32 family.


FUNCTION: Probable mitochondrial adenylate carrier that catalyzes the transport of ATP, ADP and AMP. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Esterase that catalyzes the deacetylation of acetyl-(R)- mandelate (in vitro). Can also hydrolyze acetyl glycolate, but with lower efficiency. Has very low N-acetyl-D-amino acid deacetylase activity with N-acetyl-D-serine and N-acetyl-D-threonine (in vitro). Theoretical substrate docking studies suggest that other N-acetylated amino acids may optimally occupy the active site and may in fact be the physiological substrates. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Atu3266/EF_0837 deacetylase family.


FUNCTION: Component of the BBSome complex (By similarity). The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function (By similarity). Required for proper BBSome complex assembly and its ciliary localization (PubMed:22922713). Required for cilia biogenesis and both the assembly and movement of intraflagellar transport proteins along the ciliary axoneme (PubMed:15231740, PubMed:22022287, PubMed:22922713). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, cilium axoneme.


FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.


FUNCTION: Inhibits the SpoIVB zymogen from undergoing autocatalytic activation by an unknown mechanism, and in this way plays a role in the sigma-K checkpoint of sporulation. SUBCELLULAR LOCATION: Forespore intermembrane space.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.


FUNCTION: Probably involved in translation. SIMILARITY: Belongs to the SUI1 family.


FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HAM1 NTPase family.


FUNCTION: ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.


FUNCTION: May be involved in the transport of PQQ or its precursor to the periplasm, in association with PQQ biosynthesis, but is not absolutely required for this synthesis. SIMILARITY: Belongs to the PqqB family.


FUNCTION: DNA ligase, which is expressed in the early stage of lytic development, has been implicated in T4 DNA synthesis and genetic recombination. It may also play a role in T4 DNA repair. SIMILARITY: Belongs to the ATP-dependent DNA ligase family.


FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. SUBCELLULAR LOCATION: Apical cell membrane. Cytoplasm. Membrane. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome. Colocalized with SHANK2 to the apical membrane of colonic crypt cells. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.


FUNCTION: Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.


FUNCTION: Promotes chloroplast protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.


SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily.


FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:22633490, PubMed:24269233). Plays an important role in fatty acid metabolism in brain and the acyl- CoAs produced may be utilized exclusively for the synthesis of the brain lipid. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type III membrane protein Peroxisome membrane; Single-pass type III membrane protein Microsome membrane; Single-pass type III membrane protein Endoplasmic reticulum membrane; Single-pass type III membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


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


FUNCTION: Reduces achiral isoflavones to chiral isoflavanones during the biosynthesis of chiral pterocarpan phytoalexins. The reduction product (sophrol) is a third isomer, which represents the penultimate intermediate in the synthesis of the phytoalexin (+)-pisatin, the major phytoalexin in pea. SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily.


FUNCTION: Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-insensitive subfamily.


FUNCTION: Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Note=Associated with kinetochores. SIMILARITY: Belongs to the NUF2 family.


FUNCTION: Nuclease involved in DNA non-homologous end joining (NHEJ); required for double-strand break repair and V(D)J recombination (PubMed:11336668, PubMed:11955432, PubMed:12055248, PubMed:14744996, PubMed:15071507, PubMed:15574326, PubMed:15936993). Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments (PubMed:11336668, PubMed:11955432, PubMed:14744996). V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs) (PubMed:11336668, PubMed:11955432, PubMed:14744996). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends (PubMed:11336668, PubMed:11955432, PubMed:14744996). These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively (PubMed:11336668, PubMed:11955432, PubMed:14744996). This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC (PubMed:15071507, PubMed:15574326, PubMed:11955432, PubMed:15936993). The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint (PubMed:11955432). Also required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ (PubMed:15456891, PubMed:15468306, PubMed:15574327, PubMed:15811628). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL) family.


FUNCTION: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts (PubMed:16765617). The geranylgeranyl diphosphate (GGPP) synthase ltmG is proposed to catalyze the first step in lolitrem biosynthesis (PubMed:16765617, PubMed:15991026). LtmG catalyzes a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (PubMed:16765617, PubMed:15991026). GGPP then condenses with indole-3- glycerol phosphate to form 3-geranylgeranylindole, an acyclic intermediate, to be incorporated into paxilline (PubMed:16765617). Either ltmG or ltmC could be responsible for this step, as both are putative prenyl transferases (PubMed:16765617). The FAD-dependent monooxygenase ltmM then catalyzes the epoxidation of the two terminal alkenes of the geranylgeranyl moiety, which is subsequently cyclized by ltmB, to paspaline (PubMed:16765617, PubMed:15991026). The cytochrome P450 monooxygenases ltmQ and ltmP can sequentially oxidize paspaline to terpendole E and terpendole F (PubMed:22750140). Alternatively, ltmP converts paspaline to an intermediate which is oxidized by ltmQ to terpendole F (PubMed:22750140). LtmF, ltmK, ltmE and ltmJ appear to be unique to the epichloe endophytes (PubMed:16765617, PubMed:15991026). The prenyltransferase ltmF is involved in the 27-hydroxyl-O-prenylation (PubMed:22750140). The cytochrome P450 monooxygenase ltmK is required for the oxidative acetal ring formation (PubMed:22750140). The multi- functional prenyltransferase ltmE is required for C20- and C21- prenylations of the indole ring of paspalanes and acts together with the cytochrome P450 monooxygenase ltmJ to yield lolitremanes by multiple oxidations and ring closures (PubMed:22750140). The stereoisomer pairs of lolitriol and lolitrem N or lolitrem B and lolitrem F may be attributed to variations in the way in which ring closure can occur under the action of ltmJ (PubMed:22750140). While the major product of this pathway is lolitrem B, the prenyl transferases and cytochrome P450 monooxygenases identified in this pathway have a remarkable versatility in their regio- and stereo-specificities to generate a diverse range of metabolites that are products of a metabolic grid rather than a linear pathway (PubMed:22750140). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the paxB family.


FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre- mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) binds directly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran- GDP) and targets Rev to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm. SUBCELLULAR LOCATION: Host nucleus, host nucleolus Host cytoplasm Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm. SIMILARITY: Belongs to the HIV-1 REV protein family.


SIMILARITY: Belongs to the UPF0306 family.


SIMILARITY: Belongs to the iron-sulfur dependent L-serine dehydratase family.


FUNCTION: G-protein coupled receptor for cannabinoids (By similarity). Mediates many cannabinoid-induced effects in the central nervous system (CNS), as well as in peripheral tissues (By similarity). Regulates cellular respiration and energy production in response to cannabinoids (By similarity). Signaling typically involves reduction in cyclic AMP (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Mitochondrion outer membrane Cell projection, axon Presynapse Note=Unexpectedly, in the mitochondria, the C-terminus is located in the mitochondrial intermembrane space, a compartment topologically considered as extracellular. In canonical seven-transmembrane G-protein coupled receptors, the C-terminus is cytosolic. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by creating a repressive structure at the core histone gene promoter (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the RTT106 family.


FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C- terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly. The viral progenies exit the cells by lytic release (By similarity). SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.


FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.


FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M43B family.


FUNCTION: 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.


FUNCTION: Methyltransferase involved in the biosynthesis of methyl anthranilate in response to stresses. Utilizes anthranilic acid as substrate. Produces exclusively the O-methyl ester. Can also use benzoic acid as substrate. Low activity with salicylic acid. SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family. SABATH subfamily.


FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.


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: Catalyzes the transport of 2-oxoglutarate (alpha- oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (By similarity). Involved in the regulation of apoptosis (PubMed:21448454). Helps protect from cytotoxic-induced apoptosis by modulating glutathione levels in mitochondria (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Catalytic subunit of an S-adenosyl-L-methionine-dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM11 methyltransferase family.


FUNCTION: Probable receptor, which is involved in the internalization of lipophilic molecules and/or signal transduction. May be involved in the uptake of lipoprotein APOE in liver (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Membrane, coated pit. SIMILARITY: Belongs to the LDLR family.


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


FUNCTION: Calcium-selective channel required to prevent calcium stores from overfilling. Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMCO1 family.


FUNCTION: Testis-specific component of the ribosome, which is required for the transition from prophase to metaphase in male meiosis I (By similarity). Compensates for the inactivated X-linked RPL10 paralog during spermatogenesis. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL16 family.


FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. pH-dependent Ca(2+) sensor required to activate the CatSper channel. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization. Associates with the CatSper complex via direct interaction with CATSPERZ, and senses intracellular Ca(2+). Together with CATSPERZ, associates with the CatSper channel pore and is required for the two-row structure of each single CatSper channel. SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium, flagellum Note=Localizes to the principal piece of the sperm tail.


FUNCTION: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG) to alpha-ketoglutarate and couples to the respiratory chain by feeding electrons from the reaction into the membrane quinone pool. Functions in a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological (PubMed:34555022). SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the L2HGDH family.


FUNCTION: An L-glutamate ligase that catalyzes the ATP-dependent post- translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH. SIMILARITY: Belongs to the RimK family.


FUNCTION: May play a role in regeneration of skeletal muscle. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


SIMILARITY: Belongs to the histidinol dehydrogenase family.


FUNCTION: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Plays an essential role in early steps of chloroplast development. May be involved in the redox control of plastid gene expression by maintening the redox state around chloroplast nucleoids. May positively regulate plastid-encoded RNA polymerase (PEP) activity, through binding to FSD2. SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid.


SIMILARITY: Belongs to the peptidase M76 family.


FUNCTION: Component of the Polycomb group (PcG) multiprotein BCOR complex, a complex required to maintain the transcriptionally repressive state of some genes, such as BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. Transcriptional repressor that may be targeted to the DNA by BCL6; this transcription repressor activity may be related to PKC signaling pathway. Represses CDKN1A expression by binding to its promoter, and this repression is dependent on the retinoic acid response element (RARE element). Promotes cell cycle progression and enhances cell proliferation as well. May have a positive role in tumor cell growth by down-regulating CDKN1A. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Within the PRC1-like complex, regulates RNF2 ubiquitin ligase activity. Regulates the expression of DPPA4 and NANOG in the NT2 embryonic carcinoma cells. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Non-specific phospholipase C (PLC) which assumes minor PLC activity during inorganic phosphate starvation. Can hydrolyze both phosphatidylcholine (PC) and phosphatidylethanolamine (PE). Required for normal accumulation of digalactosyldiacylglycerol (DGDG) during phosphate limitation and may contribute to the conversion of phospholipids to diacylglycerol, the substrate for galactolipid synthesis. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the bacterial phospholipase C family.


FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate. SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.


SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain family.


FUNCTION: Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (PubMed:23791524, PubMed:25938945, PubMed:31043717) (By similarity). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5- InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (PubMed:27080106). FUNCTION: (Microbial infection) Confers susceptibility to xenotropic murine leukemia retrovirus (X-MLV) infection in vitro. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family.


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


FUNCTION: May play a role into cellular response to oxidative stress. May decrease cell proliferation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EIF1AD family.


FUNCTION: [Antimicrobial peptide 1.1a]: Antimicrobial peptide active against the fungus A.alternata (IC(50)=8.6 uM) and the oomycetes P.infestans OSV 12 (IC(50)=11 uM) and P.infestans PRILL 2 (IC(50)=6.5 uM).


FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1D-myo-inositol 3- phosphate in a NAD-dependent manner. SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.


FUNCTION: In the wool cortex, wool keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated proteins (KRTAP), which are essential for the formation of a rigid and resistant wool shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of wool keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SIMILARITY: Belongs to the KRTAP type 3 family.


FUNCTION: Antiporter that transports inorganic anions (sulfate, sulfite, thiosulfate and phosphate) and, to a lesser extent, a variety of dicarboxylates (e.g. malonate, malate and citramalate) and, even more so, aspartate. The sulfate/sulfate exchange is much higher than the phosphate/phosphate and malate/malate exchanges. The transport affinities is higher for sulfate and thiosulfate than for any other substrate. May catalyze the export of sulfite and thiosulfate (the hydrogen sulfide degradation products) from the mitochondria, thereby modulating the level of the hydrogen sulfide. Also may mediate a very low unidirectional transport of sulfate. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


SUBCELLULAR LOCATION: Membrane.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.


FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). May indirectly enhance GAP-43 expression by binding to the NGF-regulatory region of its mRNA. FUNCTION: Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-62 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase. May indirectly enhance GAP-43 expression by binding to the NGF- regulatory region of its mRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the endosulfine family.


FUNCTION: Allows to use formate as major electron donor during anaerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the formate dehydrogenase gamma subunit family.


FUNCTION: May mediate the import of long-chain fatty acids (LCFA) by facilitating their transport across cell membranes (PubMed:20448275, PubMed:20530735). Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:10479480). Mainly functions as a bile acyl-CoA synthetase catalyzing the activation of bile acids via ATP-dependent formation of bile acid CoA thioesters which is necessary for their subsequent conjugation with glycine or taurine (PubMed:10749848, PubMed:11980911). Both primary bile acids (cholic acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and lithocholic acid) are the principal substrates (PubMed:10749848, PubMed:11980911). In vitro, activates 3-alpha,7-alpha,12-alpha- trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy- 5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol (PubMed:11980911). Plays an important role in hepatic fatty acid uptake and bile acid reconjugation and recycling but not in de novo synthesis of bile acids (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Microsome Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Constitutes one of the two catalytic subunit of the tRNA- splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body. Probably carries the active site for 5'-splice site cleavage. The tRNA splicing endonuclease is also involved in mRNA processing via its association with pre-mRNA 3'-end processing factors, establishing a link between pre-tRNA splicing and pre-mRNA 3'-end formation, suggesting that the endonuclease subunits function in multiple RNA-processing events (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Note=May be transiently localized in the nucleolus. SIMILARITY: Belongs to the tRNA-intron endonuclease family.


FUNCTION: Seems to be required for the LH-II stabilization.


FUNCTION: Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity). PCP is maintained by two molecular modules, the global and the core modules, PRICKLE3 being part of the core module (By similarity). Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity). Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). Required for proper assembly, stability, and function of mitochondrial membrane ATP synthase (mitochondrial complex V) (PubMed:32516135). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion Note=Recruited by VANGL2 to anterior cell borders. This polarity is controlled by Wnt proteins (By similarity). WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity). SIMILARITY: Belongs to the prickle / espinas / testin family.


FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Could catalyze the production of N(omega)- hydroxy-L-arginine (NHA) from L-arginine. SIMILARITY: Belongs to the DcsA family.


FUNCTION: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly. FUNCTION: The secreted form acts as an enterotoxin that causes phospholipase C-dependent elevation of the intracellular calcium concentration in host intestinal mucosa cells. Increased concentration of intracellular calcium disrupts the cytoskeleton and the tight junctions, raising the paracellular permeability. Potentiates chloride ion secretion through a calcium ion-dependent signaling pathway, inducing age-dependent diarrhea. To perform this enterotoxigenic role in vivo, NSP4 is released from infected enterocytes in a soluble form capable of diffusing within the intestinal lumen and interacting with host plasma membrane receptors on neighboring epithelial cells such as integrins ITGA1/ITGB1 and ITGA2/ITGB1. SUBCELLULAR LOCATION: Host rough endoplasmic reticulum membrane; Single-pass type III membrane protein Host membrane, host caveola; Single-pass type III membrane protein Secreted Note=NSP4 localizes also in vesicular structures which contain autophagosomal markers and associate with viroplasms in virus- infected cells. Additionally, a soluble form of glycosylated NSP4 is secreted despite retention of its transmembrane domain. SIMILARITY: Belongs to the rotavirus NSP4 family.


FUNCTION: Post-meiotically transcribed gene that has a role in late spermiogenesis; required for actin cone progression during spermatid individualization. SIMILARITY: Belongs to the male-specific scotti family.


SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family.


FUNCTION: Anion-transporting ATPase. Catalyzes the extrusion of arsenite (By similarity). SIMILARITY: Belongs to the arsA ATPase family.


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


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


FUNCTION: Pasteurella leukotoxins are exotoxins that attack host leukocytes and especially polymorphonuclear cells, by causing cell rupture. The leukotoxin binds to the host LFA-1 integrin and induces a signaling cascade leading to many biological effects, including tyrosine phosphorylation of the CD18 tail, elevation of the intracellular Ca(2+) and lysis of the host cell (By similarity). This leukotoxin is a major contributor to the pathogenesis of lung injury in ovine pneumonic pasteurellosis. It has also weak hemolytic activity. SUBCELLULAR LOCATION: Secreted Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.


FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family. MtnA subfamily.


FUNCTION: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4- phosphate (MEP). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the DXR family.


FUNCTION: Receptor speculated to be essential for sexual development. May regulate gonadotropin-releasing hormone (GnRH) secretion. The receptor expression could be a 'stop signal' for GnRH1, GnRH2, and GnRH3 neuronal migration, leading to suppression of cell growth and modulation of GnRH secretion, which is important for normal sexual development. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA. GSPT1/ERF3A mediates ETF1/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site. GTP hydrolysis by GSPT1/ERF3A induces a conformational change that leads to its dissociation, permitting ETF1/ERF1 to accommodate fully in the A-site. Component of the transient SURF complex which recruits UPF1 to stalled ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Required for SHFL-mediated translation termination which inhibits programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and cellular genes. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. ERF3 subfamily.


FUNCTION: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cytoplasm. Note=Located mainly at the cell surface under basal conditions. Agonist stimulation results in internalization to the cytoplasm. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including RIM101 itself), mainly by repressing transcriptional repressors of those genes, and represses transcription of acid- expressed genes. Required for meiosis, sporulation and invasive growth. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pacC/RIM101 family.


FUNCTION: Regulates secA expression by translational coupling of the secM secA operon. Translational pausing at a specific Pro residue 5 residues before the end of the protein may allow disruption of a mRNA repressor helix that normally suppresses secA translation initiation. SUBCELLULAR LOCATION: Cytoplasm, cytosol Periplasm Note=The active form is cytosolic, while the periplasmic form is rapidly degraded, mainly by the tail-specific protease. SIMILARITY: Belongs to the SecM family.


FUNCTION: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.


FUNCTION: Seems to be involved in viral proteins maturation by cleavage at Ala-Gly-|-Xaa motifs. SIMILARITY: Belongs to the peptidase M44 family.


FUNCTION: Exhibits an obligate exchange activity for serine, threonine and aromatic amino acids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.


FUNCTION: Plays a role in viral cell-to-cell propagation, by facilitating genome transport to neighboring plant cells through plasmosdesmata,. SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the Tymovirales TGBp2 protein family.


FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P) and phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) (PubMed:11001925, PubMed:10900271, PubMed:12646134, PubMed:14722070). Has also been shown to dephosphorylate phosphotyrosine- and phosphoserine-containing peptides (PubMed:9537414). Negatively regulates EGFR degradation through regulation of EGFR trafficking from the late endosome to the lysosome (PubMed:14722070). Plays a role in vacuolar formation and morphology. Regulates desmin intermediate filament assembly and architecture (PubMed:21135508). Plays a role in mitochondrial morphology and positioning (PubMed:21135508). Required for skeletal muscle maintenance but not for myogenesis (PubMed:21135508). In skeletal muscles, stabilizes MTMR12 protein levels (PubMed:23818870). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein Cell projection, filopodium Cell projection, ruffle Late endosome Cytoplasm, myofibril, sarcomere Note=Localizes as a dense cytoplasmic network (PubMed:11001925). Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles (PubMed:12118066). Predominantly located in the cytoplasm following interaction with MTMR12 (PubMed:12847286). Recruited to the late endosome following EGF stimulation (PubMed:14722070). In skeletal muscles, co-localizes with MTMR12 in the sarcomere (By similarity). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily.


FUNCTION: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics. SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Multi-pass membrane protein. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG subfamily.


FUNCTION: Transcriptional repressor. May repress NR5A1, PPARG, NR1H3, NR4A2, ESR1 and NR3C1 transcriptional activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal adenylate kinase family.


FUNCTION: Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Binds 1 c-di-GMP dimer per subunit. Increasing levels of c-di-GMP lead to decreased motility. SUBCELLULAR LOCATION: Bacterial flagellum basal body. SIMILARITY: Belongs to the YcgR family.


FUNCTION: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. FUNCTION: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ArnF family. SIMILARITY: Belongs to the ArnF family.


SIMILARITY: Belongs to the glycosyl hydrolase 13 family.


FUNCTION: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53 (PubMed:11696557). Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING-based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M (By similarity). FUNCTION: Ubiquitin-like protein which plays an important role in cell cycle control and embryogenesis via its conjugation to a limited number of cellular proteins, such as cullins or p53/TP53. Attachment of NEDD8 to cullins is critical for the recruitment of E2 to the cullin-RING- based E3 ubiquitin-protein ligase complex, thus facilitating polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins. Attachment of NEDD8 to p53/TP53 inhibits p53/TP53 transcriptional activity. Covalent attachment to its substrates requires prior activation by the E1 complex UBE1C-APPBP1 and linkage to the E2 enzyme UBE2M. SUBCELLULAR LOCATION: Nucleus Note=Mainly nuclear. SUBCELLULAR LOCATION: Nucleus Note=Mainly nuclear. SIMILARITY: Belongs to the ubiquitin family.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.


FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmA/TRMU family. SIMILARITY: Belongs to the MnmA/TRMU family.


FUNCTION: Negative regulator of cell death and defense responses. Repress a number of R genes and may have effects in promoting growth and development. May function in membrane trafficking and in fusion of vesicles with plasma membrane (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the copine family.


SIMILARITY: Belongs to the NADH dehydrogenase family.


FUNCTION: Enhances conjugal transfer of the Ti plasmid. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme. SIMILARITY: Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family. MET8 subfamily.


FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)- CoA from the cytosol to the peroxisome lumen (PubMed:12176987). Coupled to the ATP-dependent transporter activity has also a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent transport into peroxisomes, the ACOT activity is essential during this transport process (By similarity). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (PubMed:25043761). Involved in several processes; namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance. Controls also the cellular response to oxidative stress by regulating mitochondrial functions such as mitochondrial oxidative phosphorylation and depolarization. And finally controls the inflammatory response by positively regulating peroxisomal beta- oxidation of VLCFAs (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein Mitochondrion membrane; Multi-pass membrane protein Lysosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.


FUNCTION: May mediate extracellular signals to regulate transcription in differentiating cells. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.


SIMILARITY: Belongs to the asfivirus H233R family.


FUNCTION: Key regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon- exon junction on mRNAs and serves as a positional landmark for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as an EJC disassembly factor, allowing translation-dependent EJC removal and recycling by disrupting mature EJC from spliced mRNAs. Its association with the 40S ribosomal subunit probably prevents a translation-independent disassembly of the EJC from spliced mRNAs, by restricting its activity to mRNAs that have been translated. Interferes with NMD and enhances translation of spliced mRNAs, probably by antagonizing EJC functions. May bind RNA; the relevance of RNA-binding remains unclear in vivo, RNA-binding was detected by PubMed:14968132, while PubMed:19410547 did not detect RNA- binding activity independently of the EJC. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm Note=Shuttles between the nucleus and the cytoplasm (PubMed:14968132). Nuclear export is mediated by XPO1/CRM1 (PubMed:14968132). SIMILARITY: Belongs to the pym family.


SIMILARITY: Belongs to the DtxR/MntR family.


FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Along with HypF, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases. HypE catalyzes the ATP-dependent dehydration of the carboxamido group attached to its C-terminal cysteine to a cyano group. SIMILARITY: Belongs to the HypE family.


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


SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type 4 family.


FUNCTION: Inactivates histamine by N-methylation. Plays an important role in degrading histamine and in regulating the airway response to histamine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. HNMT family.


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


SIMILARITY: Belongs to the RTX toxin acyltransferase family.


FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the ALYREF family.


FUNCTION: ATP transporter involved in the uptake of ATP from the host cell cytoplasm. Provides the microsporidian cell with host ATP in exchange for ADP. This is an obligate exchange system. This energy acquiring activity is an important component of microsporidian parasitism. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Only found on the surface of parasites living inside host cells. SIMILARITY: Belongs to the ADP/ATP translocase tlc family.


FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus Chromosome. SIMILARITY: Belongs to the histone H3 family.


SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the poly(A) polymerase family.


SIMILARITY: Belongs to the adhesin P1 family.


SIMILARITY: Belongs to the snRNP Sm proteins family.


FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SWEET sugar transporter family.


FUNCTION: Component of the tartrate utilization system and may allow entry of tartrate and tartrate dehydrogenase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Phthalate permease family.


FUNCTION: Transpeptidase that anchors surface proteins to the cell wall (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall (PubMed:10446208, PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224). Utilizes lipid II as the peptidoglycan substrate for the sorting reaction (PubMed:10446208, PubMed:11856734). Responsible for the display of important virulence factors (PubMed:14769030). Important for interactions with the host and host colonization during infection (PubMed:10805806, PubMed:14769030). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the bacterial sortase family. Class A subfamily.


FUNCTION: VP10 self-assembles, together with capsid protein VP4, to form an icosahedral caspid of 87 nm in diameter, with a T=43 symmetry and composed of 420 hexamers and 12 pentamers (PubMed:31636205). VP4 proteins arrange into hexons, while VP10 proteins form the pentameric densities located at the 5-fold axes in the virion (PubMed:31636205). The stoichiometry of VP4:VP10 is 42:1 (PubMed:31636205). SUBCELLULAR LOCATION: Virion.


FUNCTION: Part of the phosphate (Pho) regulon, which plays a key role in phosphate homeostasis. Encoded together with proteins of the phosphate-specific transport (Pst) system in the polycistronic pstSCAB- phoU operon. PhoU is essential for the repression of the Pho regulon at high phosphate conditions. In this role, it may bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR- PhoB transitory complex (By similarity). FUNCTION: Part of the phosphate (Pho) regulon, which plays a key role in phosphate homeostasis. Encoded together with proteins of the phosphate-specific transport (Pst) system in the polycistronic pstSCAB- phoU operon. PhoU is essential for the repression of the Pho regulon at high phosphate conditions. In this role, it may bind, possibly as a chaperone, to PhoR, PhoB or a PhoR-PhoB complex to promote dephosphorylation of phospho-PhoB, or inhibit formation of the PhoR- PhoB transitory complex. Is also part of complex networks important for bacterial virulence, tolerance to antibiotics and stress response. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PhoU family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the carbamate kinase family.


FUNCTION: Required for efficient export of polyadenylated RNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre- mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. Regulates transcriptional elongation of a subset of genes. Involved in genome stability by preventing co-transcriptional R-loop formation (By similarity). FUNCTION: Participates in an apoptotic pathway which is characterized by activation of caspase-6, increases in the expression of BAK1 and BCL2L1 and activation of NF-kappa-B. This pathway does not require p53/TP53, nor does the presence of p53/TP53 affect the efficiency of cell killing. Activates a G2/M cell cycle checkpoint prior to the onset of apoptosis. Apoptosis is inhibited by association with RB1 (By similarity). Essential for early embryonic development. Required for normal gene expression during postnatal testis development. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleoplasm Nucleus matrix Cytoplasm Note=Can shuttle between the nucleus and cytoplasm. Nuclear localization is required for induction of apoptotic cell death. Translocates to the cytoplasm during the early phase of apoptosis execution (By similarity).


FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. ATZ/TRZ family.


FUNCTION: Probably acts as a transcriptional regulator. Required for the specification of the tarsal segment. Also involved in antenna development. SUBCELLULAR LOCATION: Nucleus.


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.


SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0194 family. SIMILARITY: Belongs to the UPF0194 family.


FUNCTION: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the HAPLN family.


FUNCTION: Plant defense peptide with antifungal activity against F.oxysporum and B.cinerea. SUBCELLULAR LOCATION: Secreted Vacuole. SIMILARITY: Belongs to the DEFL family.


FUNCTION: Acts as a ligand for the urokinase plasminogen activator surface receptor. Plays a role in angiogenesis by inducing endothelial cell migration and the formation of vascular network (cords). Involved in cellular migration and adhesion. Increases the phosphorylation levels of FAK. Interacts with and increases the mitogenic activity of HGF (By similarity). Promotes synapse formation. SUBCELLULAR LOCATION: Secreted Cytoplasm Cell surface Synapse.


FUNCTION: Key enzyme in the degradation of tyrosine. SIMILARITY: Belongs to the 4HPPD family.


FUNCTION: Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis. SIMILARITY: Belongs to the aldo/keto reductase family.


SIMILARITY: Belongs to the cyclin family. Cyclin F subfamily.


FUNCTION: Mitochondrial transporter that does not mediate citrate export from mitochondria to cytoplasm (PubMed:36177470). Its exact function has still to be determined (PubMed:36177470). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Multidrug transporter that confers resistance to 5- flucytosine (5-FC) and clotrimazole (PubMed:28066366). Confers also resistance to benomyl, but not 4-nitroquinoline-N-oxide, cycloheximide, or fluconazole (PubMed:17046176). Plays direct roles in extrusion of 5- flucytosine and clotrimazole (PubMed:28066366). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Electrogenic proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides. Transports neutral and monovalently charged peptides with a proton to peptide stoichiometry of 1:1 or 2:1 (PubMed:7896779, PubMed:9835627, PubMed:8914574, PubMed:15521010, PubMed:18367661, PubMed:19685173, PubMed:26320580) (By similarity). Primarily responsible for the absorption of dietary di- and tripeptides from the small intestinal lumen (By similarity). Mediates transepithelial transport of muramyl and N-formylated bacterial dipeptides contributing to recognition of pathogenic bacteria by the mucosal immune system (PubMed:9835627, PubMed:15521010). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=Localized to the apical membrane of enterocytes. SIMILARITY: Belongs to the major facilitator superfamily. Proton- dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.


FUNCTION: Trans-prenyltransferase that acts in both the aspulvinones and butyrolactones pathways (PubMed:28791090). Prenylates aspulvinone E and butyrolactone II to yield repectively aspulvinone H and butyrolactone I (PubMed:28791090). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.


SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family.


FUNCTION: Snake venom phospholipase A2 homolog that lacks enzymatic activity (PubMed:29067765). Shows moderate cytotoxicity against C2C12 myotubes (activity above 200 ug/mL) (PubMed:29067765). Also shows antibacterial activity against both Gram-positive and Gram-negative bacteria (PubMed:29067765). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily.


FUNCTION: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family.


FUNCTION: Single-stranded DNA-binding protein required for DNA replication. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae DNA-binding protein family.


SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. SIMILARITY: Belongs to the methyl-coenzyme M reductase gamma subunit family.


FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins. SIMILARITY: Belongs to the KRTAP type 10 family.


FUNCTION: Induces the formation of specific membrane adhesion sites between the inner and outer membranes, apparently leading to host cell lysis. Lysis may be performed via activation of host murein hydrolases. SUBCELLULAR LOCATION: Host cell inner membrane; Single-pass membrane protein Host cell outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Leviviricetes lysis protein family.


SIMILARITY: Belongs to the thioesterase PaaI family.


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


FUNCTION: This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity). SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.


FUNCTION: Catalyzes the transfer of the mannosyl group from GDP-mannose to di-myo-inositol-1,3'-phosphate (DIP), producing mannosyl-di-myo- inositol phosphate (MDIP). Can also use MDIP as an acceptor of a second mannose residue, yielding di-mannosyl-di-myo-inositol phosphate (MMDIP). Minor amounts of the tri-mannosylated form are also formed. SIMILARITY: Belongs to the MDIP synthase family.


FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the polypeptide deformylase family.


FUNCTION: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aTrm56 family.


FUNCTION: Involved in cell shape and neuronal morphogenesis, positively regulating the establishment and maintenance of dendritic spines (PubMed:19812310). Plays a role in cellular protein transport, including protein transport away from primary cilia (By similarity). May function via activation of RAC1 and PAK1 (PubMed:19812310). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium.


FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Plasma kallikrein subfamily.


FUNCTION: Transcription factor specifically required to repress long interspersed nuclear element 1 (L1) retrotransposons: recognizes and binds L1 sequences and repress their expression by recruiting a repressive complex containing TRIM28/KAP1 (PubMed:25274305). Not able to repress expression of all subtypes of L1 elements. Binds to the 5' end of L1PA4, L1PA5 and L1PA6 subtypes, and some L1PA3 subtypes. Does not bind to L1PA7 or older subtypes nor at the most recently evolved L1PA2 and L1Hs. 50% of L1PA3 elements have lost the ZNF93-binding site, explaining why ZNF93 is not able to repress their expression (PubMed:25274305). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Involved in the biosynthesis of tyrosine. Has no prephenate dehydrogenase activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.


FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the AG-peptide AGP family.


FUNCTION: Together with an NADPH cytochrome P450 the enzyme system catalyzes the terminal hydroxylation as the first step in the assimilation of alkanes and fatty acids. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Interacts with and disrupts the function of host retinoblastoma-related proteins RBR, which are key regulators of the cell cycle. Induces transcriptional activation of E2F-regulated S-phase and G2/M-phase-specific genes. Inactivation of the ability of RBR to arrest the cell cycle leads to the stimulation of viral DNA replication. SIMILARITY: Belongs to the nanovirus Clink protein family.


FUNCTION: Involved in degradation of plant cell wall polysaccharides. Has acetyl esterase activity towards a broad range of substrates including xylose-tetraacetate, 4-O-methylumbelliferyl acetate, glucose- pentaacetate, cephalosporin C, and acetylated xylo-oligosaccharides smaller than xylo-heptaose. Displays no detectable activity on polymeric acetylated xylan. SIMILARITY: Belongs to the carbohydrate esterase 7 family.


SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.


FUNCTION: Plays a role in DNA repair (PubMed:9141693, PubMed:11810266). Might stabilize or process Holliday junction intermediates (PubMed:15317759). May work with DisA following methyl methanesulfonate (MMS) but not H(2)O(2) damage; DisA is a DNA integrity scanning protein with c-di-AMP synthase activity. FUNCTION: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function. SIMILARITY: Belongs to the RecA family. RadA subfamily.


FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis- acting element (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group III family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family.


FUNCTION: Protects drg1 from proteolytic degradation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ZC3H15/TMA46 family.


SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the asfivirus E184L family.


FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity). SIMILARITY: Belongs to the peptidase C19 family.


FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. 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. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family.


SIMILARITY: Belongs to the ODF3 family.


FUNCTION: The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 2 RIP subfamily.


FUNCTION: Catalyzes the cyclization of farnesyl diphosphate to multiple sesquiterpenes, such as olefins and sesquiterpene alcohols. SIMILARITY: Belongs to the terpene synthase family.


SIMILARITY: Belongs to the UPF0026 family.


FUNCTION: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA. Shows a marked preference for deproteinized 16S rRNA as substrate and is completely inactive with native 30S subunits as substrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.