FUNCTION: Magnesium transporter. FUNCTION: Acts as accessory component of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. Involved in N-glycosylation of STT3B-dependent substrates. Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with MAGT1. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Has also oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OST3/OST6 family.


FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SRP19 family.


SUBCELLULAR LOCATION: [Matrix protein p19]: Virion.


FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF4 family.


FUNCTION: DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. SUBCELLULAR LOCATION: Cytoplasm, nucleoid.


FUNCTION: Prohibitin probably acts as a holdase/unfoldase for the stabilization of newly synthesized mitochondrial proteins. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass type II membrane protein; Intermembrane side. SIMILARITY: Belongs to the prohibitin family.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 18 family.


FUNCTION: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs. SUBCELLULAR LOCATION: Plastid, chloroplast Cytoplasm.


SIMILARITY: Belongs to the ECD family.


FUNCTION: Effector protein that contributes to pathogen virulence (PubMed:29671919). Targets members of the RABA GTPases subfamily to inhibit vesicular secretion, leading to an accumulation of secretory proteins in the endoplasmic reticulum (PubMed:29671919). SUBCELLULAR LOCATION: Secreted Host cell membrane Host endomembrane system Note=The subcellular localization to plasma and vesicular membranes is most likely the result of binding of RxLR24 to membrane-localized RABA proteins. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 05 (F4a) subfamily.


FUNCTION: Could be part of a sulfur-relay system. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrE/TusD family.


FUNCTION: Acrosomal membrane-anchored protein involved in the process of fertilization and in acrosome biogenesis. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane; Single-pass type I membrane protein. Note=In the anterior acrosome region, enriched on the inner acrosomal membrane but minimal on the outer acrosomal membrane; in contrast in the posterior acrosome region enriched on both the inner and outer acrosomal membranes.


FUNCTION: Probable member of the two-component regulatory system SERP2405/SERP2406. SUBCELLULAR LOCATION: Cytoplasm.


SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family.


FUNCTION: Promotes hydrolysis of glycogen and lipids, and raises the blood sugar level. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family.


FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling downstream of the N-formylpeptide chemoattractant receptors and leukotriene receptors (PubMed:10480894). Inhibits B cell chemotaxis toward CXCL12 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form (PubMed:10480894, PubMed:18434541). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytosol.


FUNCTION: Ferredoxin-plastoquinone reductase involved in cyclic electron flow (CEF) around photosystem I. The homodimer is probably not involved in CEF. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein Note=Predominantly located in the appressed regions of the thylakoids and less abundant in the stroma lamellae. SIMILARITY: Belongs to the PGR5 family.


FUNCTION: Postsynaptic neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 02 (Hwtx-2) subfamily.


FUNCTION: Probable mitochondrial mRNA stabilization factor. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the ATP25 family.


FUNCTION: Catalyzes the formation of an amide bond between tyramine and the gamma carboxy group of L-glutamate. The enzyme also accepts phenylethylamine in vitro.


FUNCTION: Does not exhibit any ribonuclease activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pancreatic ribonuclease family.


FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. Linked to the keratinization of epithelial tissues. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell junction, desmosome.


FUNCTION: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspP family.


FUNCTION: Putative O-methyltransferase. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.


FUNCTION: Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity. The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones. In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides. In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega- hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss. In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (By similarity). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia (PubMed:23382512). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lipoxygenase family.


SIMILARITY: Belongs to the UPF0612 family.


FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. SIMILARITY: Belongs to the IUNH family. RihA subfamily.


SIMILARITY: Belongs to the carbamoyltransferase HypF family.


FUNCTION: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants (PubMed:16844780). Degrades cutin, a macromolecule that forms the structure of the plant cuticle (By similarity). Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cutinase family.


FUNCTION: Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at one or more of its N-terminal cysteine residues, which is required for its proper membrane localization. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3 subfamily.


FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways. SUBCELLULAR LOCATION: Lipid droplet Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols.


FUNCTION: Acts as a transcriptional activator that mediates transcriptional activation by binding to E box-containing promoter (5'- CANNTG-3') (PubMed:9310321, PubMed:9740021). Acts as a differentiation factor during neurogenesis (PubMed:9310321). Induces photoreceptor cell overproduction in vivo and de novo generation in vitro (PubMed:9740021). May play a role in photoreceptor cell production (PubMed:9740021). SUBCELLULAR LOCATION: Cytoplasm Nucleus.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0132 family.


FUNCTION: Its target is unknown, but this toxin may modulate voltage- activated calcium channels (Cav) or calcium-dependent potassium channels (KCa). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the O2 superfamily. Contryphan family.


FUNCTION: Involved in development of cell polarity during the cell division cycle. Required for the establishment of actin polarization in germ cells. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.


FUNCTION: Essential for development and viability. Required for ovary development and oogenesis, and is essential for the development of the indirect flight muscles. May act as a negative regulator of the Notch signaling pathway in certain tissues, such as the muscle precursors and ovaries. May function as a linker protein between the actin and microtubule cytoskeletons. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cell cortex Note=In the cytoskeleton associates with both actin and the microtubules. SIMILARITY: Belongs to the GAS2 family.


FUNCTION: Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factors 3/IRF3 and 7/IRF7, transcription factors critical for the induction of interferons alpha and beta. This blockage is produced through the inhibition of host TBK1, by binding host TBK1 adapter proteins TBKBP1 and AZI2, thereby producing a strong inhibition of the phosphorylation and activation of IRF3 and IRF7. Acts also as an inhibitor of the cellular response to type I IFN by interacting with host STAT2. Mechanistically, exerts its inhibitory effect after host ISGF3 complex (composed of STAT1, STAT2 and IRF9) binding to the interferon stimulated response element (ISRE). SIMILARITY: Belongs to the orthopoxvirus OPG029 family.


FUNCTION: Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (By similarity). Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (By similarity). Inhibits SUV39H1 methyltransferase activity (PubMed:19218236). Mediates ligand- dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (By similarity). Regulates the circadian expression of the core clock components NR1D1 and BMAL1 (PubMed:23398316). Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (By similarity). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (By similarity). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (By similarity). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (By similarity). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle Note=Recruited to chromatin, post-UV irradiation. Sequestered to the cytoplasm in the presence of MCC. Translocated to the cytoplasm during UV-induced apoptosis.


FUNCTION: This hormone from hypothalamus regulates the release of corticotropin from pituitary gland. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family.


SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the DIPK family.


FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SIMILARITY: Belongs to the GST superfamily. Phi family.


FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. May be involved in lipopolysaccharide biosynthesis, potentially channelling CTP directly to CMP-KDO synthetase (PubMed:8951811). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity). SIMILARITY: Belongs to the CTP synthase family.


FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. FUNCTION: Transforming growth factor beta-1: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency- associated peptide (LAP) and Transforming growth factor beta-1 (TGF- beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix. At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus. TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin- binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1. Once activated following release of LAP, TGF- beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency- associated peptide chain (LAP) and 'milieu molecules'. Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner (By similarity). Can induce epithelial- to-mesenchymal transition (EMT) and cell migration in various cell types (By similarity). FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1. Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1. SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix. SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted. SIMILARITY: Belongs to the TGF-beta family.


FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (By similarity). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity). Involved in microtubule glycylation of primary cilia in colon which controls cell proliferation of epithelial cells and plays an essential role in colon cancer development (PubMed:25180231). Together with TTLL8, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, cilium Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, flagellum axoneme.


FUNCTION: Involved in mycelium differentiation. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. FUNCTION: Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Rieske iron-sulfur protein family.


FUNCTION: Acts as an osmosensitive calcium-permeable cation channel. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.


FUNCTION: Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae TRX2 protein family.


SUBCELLULAR LOCATION: Secreted Note=Probably secreted via the ESX-5 / type VII secretion system (T7SS). SIMILARITY: Belongs to the WXG100 family. ESAT-6 subfamily.


FUNCTION: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRM1 family.


SIMILARITY: Belongs to the coronaviruses ns4.9 protein family.


FUNCTION: Seems to act as an inhibitor of cellular proliferation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative (PubMed:20139316, PubMed:21351751, PubMed:22730213, PubMed:22909031, PubMed:26266881). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG (PubMed:20139316). The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone (PubMed:20139316). The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751, PubMed:22909031). The short chain dehydrogenase mdpC converts the tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-thracen-1(2H)-one derivative (PubMed:22909031, PubMed:26266881). These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin (PubMed:22730213). Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps (PubMed:22730213). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 13 family.


FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.


FUNCTION: Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-222 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (By similarity). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (By similarity). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the fic family.


FUNCTION: C-24(28) sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:8125337, PubMed:18310029). Erg4 catalyzes the last step of ergosterol biosynthesis by converting ergosta-5,7,22,24(28)-tetraen- 3beta-ol into ergosterol (PubMed:8125337, PubMed:18310029). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha- demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C- 4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. Then, the sterol 24- C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl- methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5- dehydroepisterol. The C-22 sterol desaturase erg5 further converts 5- dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta- 5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (PubMed:18310029) (Probable). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (PubMed:8586261) (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERG4/ERG24 family.


FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that shows presynaptic neurotoxicity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity). FUNCTION: Heterodimer: postsynaptic neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.


FUNCTION: ATPase that stimulates 40S and 60S ribosome biogenesis (PubMed:16260602). Also involved in ribosome-associated quality control (RQC) pathway, a pathway that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation: localizes to the ribosomal E-site and stimulates VMS1-dependent tRNA cleavage (PubMed:31189955). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the cytoplasm and the nucleus. SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.


FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate. SIMILARITY: Belongs to the carbohydrate kinase PfkB family.


FUNCTION: Controls the rotational direction of flagella during chemotaxis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FliL family.


FUNCTION: Metalloprotease (By similarity). Acts together with protease sup-17 to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision (PubMed:16197940). By modulating glp-1/Notch signaling, plays a role in germline development (PubMed:16197940). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). SIMILARITY: Belongs to the SepCysS family.


SIMILARITY: To B.subtilis YxjH.


FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of three 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the trisaccharide alpha-Kdo-(2->8)-alpha-Kdo- (2->4)-alpha-Kdo. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 30 subfamily.


FUNCTION: A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein assembles into a pre-pore complex. A conformation change leads to insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host cell membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Can be reversibly inactivated by oxidation. SUBCELLULAR LOCATION: Secreted Host cell membrane; Multi-pass membrane protein Note=Secreted as soluble protein that then inserts into the host cell membrane and forms huge pores formed by transmembrane beta-strands. SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMIM13 family.


FUNCTION: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C- termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AAA ATPase family.


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


FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin- protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. SIMILARITY: Belongs to the NPH3 family.


FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA polymerase subunit family.


FUNCTION: C2H2-type zinc-finger transcription factor that controls the expression of the nonribosomal peptide synthases inpA and inpB, as well as of the other inp cluster-associated genes (PubMed:20952652, PubMed:27294372). Mediates also the expression of the asperfuranone biosynthesis gene cluster by binding to the afoA promoter (PubMed:20952652). Probably recognizes the 5'-CT/C/AAAAGGAT/AT/GG/CA-3' motif in the promoters of teget genes (PubMed:20952652). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.


SUBCELLULAR LOCATION: Secreted, cell wall Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. SIMILARITY: Belongs to the glycosyl hydrolase 17 family.


FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily.


FUNCTION: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Part of the pseudopilus tip complex that is critical for the recognition and binding of secretion substrates. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP H family.


FUNCTION: Modulates the competence to flowering of apical meristems. SIMILARITY: Belongs to the FPF1 family.


FUNCTION: Unknown. Target of pap1 transcription factor. Confers brefeldin A resistance in S.pombe. SIMILARITY: Belongs to the WrbA family.


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


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


FUNCTION: Not known; ectopic expression of LOB leads to alterations in the size and shape of leaves and floral organs and causes male and female sterility. SIMILARITY: Belongs to the LOB domain-containing protein family.


FUNCTION: 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. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. Plays a role in apoptosis negative control involved in brain development. SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the WD repeat THOC6 family.


FUNCTION: RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Involved in structural and functional organization of telomeric chromatin and regulates silencing at the HMR locus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, P-body Nucleus Chromosome, telomere. SIMILARITY: Belongs to the HEK2 family.


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


FUNCTION: Involved in peroxisomal proliferation. Promotes peroxisome division and biogenesis. SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the peroxin-11 family.


FUNCTION: May serve to lubricate the movement of the cellulose microfibrils during cell growth and wall extension and/or may serve to maintain the fluid state of the slug cell wall. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily.


FUNCTION: May constitute a glutathione peroxidase-like protective system against oxidative stresses. Involved positively in abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, seed germination and inhibition of vegetative growth. Oxidizes and represses target proteins (e.g. the phosphatase activity of ABI1 and ABI2) when oxidized by H(2)O(2), probably after ABA signaling. Modulates the calcium channel activity in guard cells in response to ABA or H(2)O(2). Confers tolerance to drought stress, by enhancing the ABA-dependent stomatal closure. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the glutathione peroxidase family.


FUNCTION: Part of an ABC transporter complex involved in carbohydrate import. Could be involved in ribose, galactose and/or methyl galactoside import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate importer 2 (CUT2) (TC 3.A.1.2) family.


FUNCTION: Probable carboxypeptidase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S10 family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family.


FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation. Shows no activity against histone H3 when it is trimethylated on 'Lys- 9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription. LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2. Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3. During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction. When secreted into the extracellular matrix, promotes cross- linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin. Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane Nucleus Chromosome Endoplasmic reticulum Note=Associated with chromatin. It is unclear how LOXL2 is nuclear as it contains a signal sequence and has been shown to be secreted. However, a number of reports confirm its intracellular location and its key role in transcription regulation. SIMILARITY: Belongs to the lysyl oxidase family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-16 family.


FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. SIMILARITY: Belongs to the FPG family.


FUNCTION: Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ZapC family.


FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the NOS 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 NdhM subunit family.


FUNCTION: Involved in maceration and soft-rotting of plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family.


FUNCTION: May act as a transporter of organic cations based on a proton efflux antiport mechanism. May play a role in the transport of chloroquine and quinidine-related compounds in kidney (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=Localized at the apical membrane surface of renal proximal tubules. SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family.


FUNCTION: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TCP-1 chaperonin family.


FUNCTION: Catalyzes the condensation of glyoxylate and glycine into (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). Functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC) (By similarity). In vitro catalyzes the cleavage of both D-erythro- and D-threo-3-hydroxyaspartate to glycine and glyoxylate. Also acts on D- threonine, D-3-phenylserine and D-3-3,4-methylenedioxyphenylserine (PubMed:12835921). SIMILARITY: Belongs to the DSD1 family.


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


FUNCTION: RNA-binding protein that may be implicated in the regulation of pre-mRNA alternative splicing. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CELF/BRUNOL family.


FUNCTION: Involved in DNA double-strand break (DSB) repair (By similarity). Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity (By similarity). SIMILARITY: Belongs to the HerA family.


FUNCTION: Receptor kinase involved in the perception of C-terminally encoded plant signaling peptide (CEP) and subsequent regulation of root and shoot development. Together with CEPR1, mediates systemic nitrogen (N)-demand signaling upon the perception of root-derived peptides (e.g. CEP1) via the up-regulation of genes involved in N uptake and assimilation pathways. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


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


FUNCTION: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicles, which are essential to create a favorable environment where Salmonella can replicate and avoid immune defenses of the host cell (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted via the type III secretion system 1 (SPI-1 TTSS). SIMILARITY: Belongs to the phosphatase IpgD/SopB family.


FUNCTION: The role of the precursor might be to condense the viral prochromatin for encapsidation by virtue of the two basic domains. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the adenoviridae pX family.


FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.


FUNCTION: Component of the sarcomeric M-band which plays a role in myocyte response to biomechanical stress (By similarity). May regulate expression of other M-band proteins via an SRF-dependent pathway (By similarity). Important for normal contractile function in heart (PubMed:20847312). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line.


FUNCTION: Pseudogene resulting from a nucleotide deletion that introduces a premature stop codon at position 66. This is the N- terminal fragment. The intact protein (AC A0A140NCB4) hydrolyzes deaminated glutathione (dGSH, 2-oxoglutaramate) to alpha-ketoglutarate (alpha-KG) and cysteinylglycine, has less activity against alpha- ketoglutaramate (a-KGM) and no activity on glutathione or L-glutamine (By similarity). May function as a metabolite repair enzyme (By similarity). SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.


FUNCTION: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers (PubMed:25078621, PubMed:28681861, PubMed:28161523, PubMed:30016436). Actively participates in the membrane fusion reaction by mediating the mixing of cell membrane lipids (hemifusion) upstream of mymx (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes on the cell surface of myoblasts. SIMILARITY: Belongs to the TMEM8 family.


FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2, IL-3, IL-4, TNF-alpha or GM-CSF. Promotes invasive migration through the activation of GPC6 expression and WNT5A signaling pathway (By similarity). Is involved in the negative regulation of chondrogenesis (PubMed:10620601). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Cytoplasmic for the phosphorylated form and nuclear after activation that is controlled by calcineurin- mediated dephosphorylation. Rapid nuclear exit of NFATC is thought to be one mechanism by which cells distinguish between sustained and transient calcium signals. The subcellular localization of NFATC plays a key role in the regulation of gene transcription.


FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNF7 family.


SUBCELLULAR LOCATION: Vacuole membrane; Single-pass type II membrane protein Note=Lysosome-like vacuoles. SIMILARITY: Belongs to the peptidase S9B family.


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


FUNCTION: Plays a role in tail tip complex assembly. The tail tip complex is assembled successively with three tail tip proteins J, one tail tip protein I, one tail tip protein L and one tail tip protein K. The tail tip complex interacts with tail measure protein to initiate tail tube assembly. The formation of the tail tip complex is completed by the addition of tail tip protein M, which is followed by tail tube polymerization. May be excluded form tail tip during maturation and would be absent from virions. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the lambda-like tail tip protein I family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-11 family.


FUNCTION: Hydrolyzes a wide range of dipeptides. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.


FUNCTION: Part of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. May act by regulating the catalytic subunit PIGA. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (PubMed:25965978). c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome, operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis. FUNCTION: Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. DisA forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation. SIMILARITY: Belongs to the DisA family.


FUNCTION: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit during ribosomal small subunit assembly. SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion inner membrane; Peripheral membrane protein. Note=Localizes on the matrix side on the mitochondrial inner membrane. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Era GTPase family.


FUNCTION: Aconitate-delta-isomerase; part of the gene cluster that mediates the biosynthesis of itaconic acid and 2-hydroxyparaconate (PubMed:26639528, PubMed:27750034). Cis-aconitate is secreted by the mitochondrial tricarboxylate transporter MTT1. In the cytosol cis- aconitate is converted into trans-aconitate via isomerization by the aconitate-delta-isomerase ADI1 (PubMed:26639528). Decarboxylation of trans-aconitate by the trans-aconitate decarboxylase TAD1 then leads then to the production of itaconic acid (PubMed:26639528). The cytochrome P450 monooxygenase CYP3 further converts itaconate to 2- hydroxyparaconate via oxidation of the double bond, leading to a transient epoxide, which can subsequently be lactonized to produce 2- hydroxyparaconate (PubMed:27750034). Secretion of itaconate and possibly 2-hydroxyparaconate into the medium is mediated by the major facilitator ITP1 (PubMed:26639528, PubMed:27750034). The glyoxalase domain-containing protein RDO1 is not involved in the biosynthesis of itaconate and 2-hydroxyparaconate, however, it might play a role in the further conversion of 2-hydroxyparaconate to itatartarate (PubMed:27750034). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the PrpF family.


FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the dickkopf family.


FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class I subfamily.


FUNCTION: Nitric oxide-responsive transcriptional regulator.


FUNCTION: Catalyzes the dehydration of aldoximes to their corresponding nitrile (PubMed:14556637). Is active toward various arylalkyl- and alkyl-aldoximes, and to a lesser extent toward aryl-aldoximes (PubMed:14556637). SIMILARITY: Belongs to the heme-containing dehydratase family.


FUNCTION: May be involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Regulates the Ca(2+)-dependent secretion of norepinephrine in PC12 cells. Required for export from the endocytic recycling compartment to the cell surface. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein Recycling endosome membrane; Single-pass membrane protein Note=In mast cells, localizes to the endocytic recycling compartment. SIMILARITY: Belongs to the synaptotagmin family.


FUNCTION: Potent inhibitor of Nav1.2/SCN2A voltage-gated sodium channels (IC(50)=0.6-0.7 nM) (PubMed:16267209, PubMed:29703751). Also weakly inhibits Nav1.1/SCN1A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.7/SCN9A and Nav1.8/SCN10A (IC(50)=20-610 nM) (PubMed:16267209, PubMed:29703751). It acts by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current (PubMed:16267209). It shows low affinity for lipid bilayers (PubMed:29703751). In vivo, this toxin causes general ataxia, lack of response to stimuli, and semiparalysis (PubMed:16267209). After a few minutes, the mice are unable to stand, and breathing is reduced in rhythm and intensity (PubMed:16267209). Symptoms gradually increase with progressive slowing of breathing and flaccid paralysis; death occurred within 10 to 20 minutes post injection (PubMed:16267209). Animals remain totally flaccid, and no symptoms of excitatory neurotoxicity are observed (PubMed:16267209). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 08 (Gtx1-15) subfamily.


FUNCTION: Hydroxyornithine transacylase; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence via intracellular iron acquisition during macrophage infection (PubMed:18404210). SUBCELLULAR LOCATION: Peroxisome Note=Targeted to peroxisomes via its PTS1-type peroxisomal targeting signal (By similarity). SIMILARITY: Belongs to the lysine N-acyltransferase mbtK family.


FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the transferrin family.


FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32), 2'O-methylated uridine (Um32) or 2'O-methylated adenosine (Am32) at position 32 in tRNA. Confers resistance to oxidative stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.


FUNCTION: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of ctnnb1-A and possibly ctnnb1-B, and as an activator in the presence of these proteins. Required early in development for the establishment of the dorsal body axis in response to maternal Wnt signaling. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TCF/LEF family.


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


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


FUNCTION: Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. SIMILARITY: Belongs to the LutA/YkgE family.


FUNCTION: Component of MIOREX complexes, large expressome-like assemblies of ribosomes with factors involved in all the steps of post- transcriptional gene expression (PubMed:25683707). Component of a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis (PubMed:25631044). SUBCELLULAR LOCATION: Mitochondrion.


FUNCTION: Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase S14 family.


FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of the acidic amino terminus of processed forms of beta- and gamma-actin (ACTB and ACTG, respectively) (PubMed:30028079, PubMed:29581253). N-terminal acetylation of processed beta- and gamma- actin regulates actin filament depolymerization and elongation (PubMed:29581253). In vivo, preferentially displays N-terminal acetyltransferase activity towards acid N-terminal sequences starting with Asp-Asp-Asp and Glu-Glu-Glu (PubMed:30028079, PubMed:29581253). In vitro, shows high activity towards Met-Asp-Glu-Leu and Met-Asp-Asp-Asp (PubMed:10644992, PubMed:29581307). May act as a tumor suppressor (PubMed:10644992). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the acetyltransferase family.


FUNCTION: Catalyzes the aldol-type condensation of 2-oxoglutarate with acetyl-CoA to yield homocitrate. Carries out the first step of the alpha-aminoadipate (AAA) lysine biosynthesis pathway. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. Homocitrate synthase LYS20/LYS21 subfamily.


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


FUNCTION: Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Is a critical central regulator of gonadal function (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the tachykinin family.


FUNCTION: Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy- inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm. Nuclear export requires functional XPO1.


FUNCTION: Potent antibacterial activity against the Gram-negative bacterium E.coli ML-35, and against the Gram-positive bacterium L.monocytogenes EGD. Lacks antifungal activity against C.albicans. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. SIMILARITY: Belongs to the beta-defensin family.


SIMILARITY: Belongs to the ZC2HC1 family.


SIMILARITY: In the C-terminal section; belongs to the prokaryotic molybdopterin-containing oxidoreductase family.


FUNCTION: Hemoglobin epsilon chain is a beta-type chain found in early embryos. SIMILARITY: Belongs to the globin family.


FUNCTION: Involved in sequestration of excess metal in the cytoplasm into vacuoles to maintain metal homeostasis. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family. SLC30A subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily.


SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S26 family.


FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (By similarity). SUBCELLULAR LOCATION: Virion Host membrane; Single-pass membrane protein. Note=prior to assembly, the major capsid protein is found associated with the bacterial host inner membrane. SIMILARITY: Belongs to the inovirus capsid protein family.


FUNCTION: Fallaxidin-3.1 shows antibacterial activity against the Gram- positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=100 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram- negative bacteria E.cloacae and E.coli. FUNCTION: Fallaxidin-3.2 shows antibacterial activity against the Gram- positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=500 uM). No antibacterial activity against the Gram-positive bacteria B.cereus, L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram- negative bacteria E.cloacae and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.


FUNCTION: Binds single-stranded DNA at the primosome assembly site (PAS). SIMILARITY: Belongs to the PriB family.


FUNCTION: Required for normal vault structure. Vaults are multi-subunit structures that may act as scaffolds for proteins involved in signal transduction. Vaults may also play a role in nucleo-cytoplasmic transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent activation of JAK. Down-regulates SRC activity and signaling through MAP kinases (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Probable B cell-associated cytokine that plays a role in the regulation of humoral immune responses (PubMed:28978694). Involved in lymphocyte B cell development and immunoglobulin/IgA production (PubMed:28978694). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of 3-oxo- tetronate to 3-oxo-tetronate 4-phosphate. SIMILARITY: Belongs to the four-carbon acid sugar kinase family.


FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity) (PubMed:22820017, PubMed:15769935, PubMed:20410296). Plays an important role in ascorbic acid biosynthesis by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone (PubMed:20410296, PubMed:15769935, PubMed:22820017). Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic (By similarity). Involved in the detoxification of lipid- derived aldehydes like acrolein (By similarity). Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity). Displays no reductase activity towards retinoids (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Apical cell membrane. SIMILARITY: Belongs to the aldo/keto reductase family.


FUNCTION: Non-regulatory myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function.


FUNCTION: Antiapoptotic factor that may have a role in protein assembly. Negatively regulates ACIN1. By binding to ACIN1, it suppresses ACIN1 cleavage from CASP3 and ACIN1-mediated DNA fragmentation. Also known to efficiently suppress E2F1-induced apoptosis (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly nuclear. SIMILARITY: Belongs to the API5 family.


FUNCTION: Catalyzes phosphatidylcholine biosynthesis from CDP-choline. It thereby plays a central role in the formation and maintenance of vesicular membranes. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family.


FUNCTION: Has a post-transcriptional repressor function in flagellum biogenesis. Associates with the 5'-UTR of fljK mRNA and promotes its degradation. SIMILARITY: Belongs to the FlbT family.


FUNCTION: Maximin-5 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. The only exception is the resistance of E.coli. Shows also antimicrobial activity against fungi C.albicans, A.flavus and P.uticale. It has little hemolytic activity. It does not possess a significant cytotoxicity against tumor cell lines. It does not possess a significant anti-HIV activity. FUNCTION: Maximin-H4 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily.


FUNCTION: Required for the normal development of the wing and halter imaginal disks. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Myotropic peptides that enhance both the frequency and amplitude of spontaneous hindgut contractions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the orcokinin family.


FUNCTION: ATPase that regulates mitochondrial ABC transporters ABCB7, ABCB8/MITOSUR and ABCB10. Regulates mitochondrial ferric concentration and heme biosynthesis and plays a role in the maintenance of mitochondrial homeostasis and cell survival. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion.


FUNCTION: Catalyzes the conversion of dTMP to dTDP. SIMILARITY: Belongs to the thymidylate kinase family.


SIMILARITY: Belongs to the UPF0377 family.


FUNCTION: Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding (By similarity). SUBCELLULAR LOCATION: Cytoplasm Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.


FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity (PubMed:12711671, PubMed:32075755). Specifically involved in tRNA repair: acts downstream of the ribosome- associated quality control (RQC) pathway by removing a 2',3'-cyclic phosphate from tRNAs following cleavage by ANKZF1 (PubMed:32075755). tRNAs are then processed by TRNT1 (PubMed:32075755). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=Mainly cytosolic. SIMILARITY: Belongs to the RNase Z family.


SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family.


FUNCTION: Catalyzes the reversible oxidation of CO(2) and methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme is oxygen-labile. SIMILARITY: Belongs to the FwdC/FmdC family.


FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the HMBS family.


FUNCTION: Heterodimerizes with IL12B to form the IL-12 cytokine or with EBI3/IL27B to form the IL-35 cytokine. IL-12 is primarily produced by professional antigen-presenting cells (APCs) such as B-cells and dendritic cells (DCs) as well as macrophages and granulocytes and regulates T-cell and natural killer-cell responses, induces the production of interferon-gamma (IFN-gamma), favors the differentiation of T-helper 1 (Th1) cells and is an important link between innate resistance and adaptive immunity. Mechanistically, exerts its biological effects through a receptor composed of IL12R1 and IL12R2 subunits. Binding to the receptor results in the rapid tyrosine phosphorylation of a number of cellular substrates including the JAK family kinases TYK2 and JAK2. In turn, recruited STAT4 gets phosphorylated and translocates to the nucleus where it regulates cytokine/growth factor responsive genes (By similarity). As part of IL- 35, plays essential roles in maintaining the immune homeostasis of the liver microenvironment and functions also as an immune-suppressive cytokine (By similarity). Mediates biological events through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers. Signaling requires the transcription factors STAT1 and STAT4, which form a unique heterodimer that binds to distinct DNA sites (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily.


FUNCTION: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys- 48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. May also promote the formation of 'Lys- 63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating ubc13-mms2 (ube2n-ube2v2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress. SUBCELLULAR LOCATION: Nucleus, PML body. SIMILARITY: Belongs to the CHFR family.


FUNCTION: Plays a role in efficient localization of neo-synthesized capsids to nuclear replication compartments, thereby controlling cleavage and packaging of virus genomic DNA. SUBCELLULAR LOCATION: Host cytoplasm. Host nucleus. SIMILARITY: Belongs to the herpesviridae UL32 protein family.


FUNCTION: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of sordarial, a salicylic aldehyde structurally related to the phytotoxin pyriculol (PubMed:19277664, PubMed:28485098, PubMed:30908040). The most interesting aspect of this pathway is formation of an aromatic product from the highly reducing polyketide synthase srdA (PubMed:30908040). SrdA synthesizes a reduced polyketide chain from one molecule of acetyl-CoA and five molecules of malonyl-CoA (PubMed:30908040). The polyketide chain is then reductively released as an aldehyde (PubMed:30908040). The oxidoreductases srdC, srdD and srdE then oxidize one of the hydroxy groups to facilitate the intramolecular aldol condensation, followed by dehydration to yield a salicylic aldehyde (PubMed:30908040). This aldehyde can undergo facile reduction by endogenous reductases to yield the alcohol 1-hydroxy-2- hydroxymethyl-3-pent-1,3-dienylbenzene (PubMed:30908040). The flavin- dependent srdI counteract against the propensity of the aldehydes to be reduced under physiological conditions and is responsible for reoxidizing 1-hydroxy-2-hydroxymethyl-3-pent-1,3-dienylbenzene back to the salicylic aldehyde (PubMed:30908040). This salicylic aldehyde is then selectively epoxidized by the cupin-domain-containing oxidoreductase srdB to yield the epoxide, which can be hydrolyzed stereoselectively by the hydrolase srdG to give the final product sordarial (PubMed:30908040). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA). FUNCTION: Hydrolyzes indole-3-acetamide (IAM) into indole-3-acetic acid (IAA). SIMILARITY: Belongs to the amidase family.


FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP (PubMed:20940301). This protein participates in processes of transmission and amplification of the visual signal. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cell projection, cilium, photoreceptor outer segment. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFA2 subunit family.


FUNCTION: Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation (By similarity). FUNCTION: Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation. SUBCELLULAR LOCATION: Cytoplasm Note=Shuttles between the lateral wall and the division site in a cell cycle-dependent manner. SUBCELLULAR LOCATION: Cytoplasm Note=Shuttles between the lateral wall and the division site in a cell cycle-dependent manner. SIMILARITY: Belongs to the GpsB family.


FUNCTION: Involved in heme (porphyrin) scavenging. Binds Fe(2+) and Fe(3+) heme but the largest fraction is Fe(2+) heme. Functions as a high-affinity heme binding protein and probably has a role in relaying heme-iron from cell wall-anchored isd proteins receptors to the probable permease IsdF (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 8 family.


FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. The small Rab GTPase RAB11A regulates endocytic recycling (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Recycling endosome membrane; Lipid-anchor Cleavage furrow Cytoplasmic vesicle, phagosome Cytoplasmic vesicle membrane. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Microbicidal activity and inhibits corticotropin (ACTH) stimulated corticosterone production. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family.


FUNCTION: Specifically catalyzes the N1-methylation of pseudouridine at position 54 (Psi54) in tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. TrmY family.


FUNCTION: Modulates the synthesis of GlmS, by affecting the processing and stability of the regulatory small RNA GlmZ. When glucosamine-6- phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ and targets it to cleavage by RNase E. Consequently, GlmZ is inactivated and unable to activate GlmS synthesis. Under low GlcN6P concentrations, RapZ is sequestered and inactivated by an other regulatory small RNA, GlmY, preventing GlmZ degradation and leading to synthesis of GlmS. SIMILARITY: Belongs to the RapZ-like family. RapZ subfamily.


FUNCTION: Catalyzes the transfer of the amino group of L-glutamate to [LysW]-aminoadipate 6-semialdehyde, generating [LysW]-gamma-L-lysine (Probable). In vitro, can use N(2)-acetyl-L-ornithine and N(2)-acetyl- L-lysine (PubMed:11489859). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. LysJ subfamily.


FUNCTION: Probable disease resistance (R) protein. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the plant RPW8 protein family.


FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. In plants, may have a detoxification role against certain herbicides (By similarity). SIMILARITY: Belongs to the GST superfamily. Phi family.


FUNCTION: ATP-dependent specificity component of the mitochondrial Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ClpX chaperone family.


FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the dynein light intermediate chain family.


FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the AccD/PCCB family.


FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (- COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.


FUNCTION: Probable transcription factor that plays a role in configuring the spinal circuits controlling stride in vertebrates. Involved in neuronal specification within a specific subdivision of spinal cord neurons and in the development of a coordinated locomotor network controlling limb movements. May regulate transcription during sexual development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DMRT family.


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


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


FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N- exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Note=May also localize to the nuclear envelope. SIMILARITY: Belongs to the EMC2 family.


FUNCTION: Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto-oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress- induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro- inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury (By similarity). Phosphorylates TRIM7 at 'Ser-107' in response to growth factor signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin ligase activity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily.


FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Is active on mammals and bind with high affinity to rat brain synaptosome. Does not display phospholipid-binding activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection (PubMed:17216664, PubMed:19067514, PubMed:20575135, PubMed:34903054). TenA catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to the production of pretenellin B and pyridovericin, respectively (PubMed:19067514, PubMed:34903054). The pathway begins with the assembly of the polyketide-amino acid backbone by the hybrid PKS-NRPS tenS with the help of the enoyl reductase tenC. These enzymes catalyze the synthesis of the pyrrolidine-2-dione intermediates pretellinin A, 11-hydropretellenin A, 12-hydropretellenin A, 13- hydropretellenin A, 14-hydropretellenin A, 12-oxopretellenin A and prototellinin D. The cytochrome P450 monooxygenase tenA then catalyzes an oxidative ring expansion of pretenellin A and 14-hydropretellenin A to form the 2-pyridone core, leading to pretenellin B and pyridovericin, respectively. The cytochrome P450 monooxygenase tenB is then required for the selective N-hydroxylation of the 2-pyridone nitrogen of yield tellinin and 15-hydroxytellenin (15-HT), respectively. The UDP-glucosyltransferase GT1 and the methyltransferase MT1, located outside the tenS gene cluster, contribute to the stepwise glycosylation and methylation of 15-HT to obtain the glycoside pyridovericin-N-O-(4-O-methyl-beta-D-glucopyranoside) (PMGP). Additional related compounds such as 1-O-methyl-15-HT, (8Z)-1-O-methyl- 15-HT, and O-methyltenellin A are also produced but the enzymes involved in their biosynthesis have still to be determined (PubMed:34903054). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re- epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways. SUBCELLULAR LOCATION: Secreted.


FUNCTION: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Required for binding the 5'- ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA (PubMed:18438418). Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs. In vitro, does not have sequence specificity. In vitro, has weak DNA exonuclease activity. In vitro, shows biphasic kinetics such that there is rapid hydrolysis of the last three unpaired RNA nucleotides in the 39 flanking sequence followed by a much slower cleavage through the stem that occurs over a longer incubation period in the order of hours (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nucleolus.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. ABL subfamily.


FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). The type III-A Csm effector complex binds crRNA and acts as a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA cognate to the crRNA is required for all activities. In a heterologous host the appropriately targeted Csm effector complex prevents growth of dsDNA phage phiNM1-gamma6. FUNCTION: This subunit has the target ssRNA endonuclease activity; it cleaves multiple sites in the target RNA at 6 nucleotide intervals. SIMILARITY: Belongs to the CRISPR-associated Csm3 family.


FUNCTION: Negatively regulates the Hedgehog (SHH) signaling. Binds to the promoter of the SHH signaling mediator, GLI1, and inhibits its expression. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm Nucleus Note=Both detected in the nucleus and cytoplasm, localizes to the nucleus where it binds chromatin upon stimulation of the Hedgehog pathway. SIMILARITY: Belongs to the actin family.


FUNCTION: Probable metal transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP (TC 2.A.55) family.