FUNCTION: Binds tightly to dsDNA (PubMed:10844682). Acts as a global transcriptional regulator through its ability to bind to AT-rich DNA sequences (PubMed:1423593, PubMed:16933988, PubMed:21673140). Binds in the minor groove of AT-rich DNA (PubMed:21673140). Was found to bind 746 genes, about half of which show no change in expression in disruption experiments suggesting these sites are important for nucleoid structure (PubMed:16933988). On a global level genes bound by H-NS are expressed at a lower than average level; H-NS is excluded from binding to highly transcribed genes and does not co-localize with RNA polymerase in DNA-binding studies during exponential growth in rich medium (PubMed:16933988). The best correlation for H-NS binding is AT- content rather than predicted DNA curvature (PubMed:16933988). Has a strong preference for DNA that has been recently acquired by horizontal gene transfer, binding strongly to Salmonella pathogenicity islands 1 and 2 (SPI1 and SPI2); this offers the selective advantage of silencing foreign DNA while keeping it in the genome in case of need (PubMed:16933988). DNA-binding influences plasmid DNA topology (PubMed:1423593). For the proU locus (the proV-proW-proX operon) inhibits transcription at low osmolarity by binding to AT-rich, curved, DNA downstream of the transcription start site of proV; repression is greater when more than 1 curved DNA sequence is present (PubMed:1423593). It plays a role in the thermal control of pili production (By similarity). It is subject to transcriptional auto- repression (By similarity). It binds preferentially to the upstream region of its own gene recognizing two segments of DNA on both sides of a bend centered around -150 (By similarity). FUNCTION: A DNA-binding protein implicated in transcriptional repression and chromosome organization and compaction. Binds nucleation sites in AT-rich DNA and bridges them, forming higher-order nucleoprotein complexes and condensing the chromosome. As many horizontally transferred genes are AT-rich, it plays a central role in silencing foreign genes. A subset of genes are repressed by H-NS in association with other proteins (By similarity). FUNCTION: A DNA-binding protein implicated in transcriptional repression (PubMed:19521501) and chromosome organization and compaction. Modifies gene expression, regardless of whether the gene is chromosomal or was acquired by horizontal gene transfer (PubMed:19521501). Binds nucleation sites in AT-rich DNA and bridges them, forming higher-order nucleoprotein complexes and condensing the chromosome. As many horizontally transferred genes are AT-rich, it plays a central role in silencing foreign genes. A subset of genes are repressed by H-NS in association with Hha and/or Cnu (ydgT) (By similarity). FUNCTION: A DNA-binding protein implicated in transcriptional repression and chromosome organization and compaction. Binds AT-rich DNA, repressing its transcription; about 754/4438 tested genes (15%) bind to H-NS, 70% of these are AT-rich and correspond to horizontally transferred geness (HTG), thus playing a central role in silencing foreign genes (PubMed:16763111). This offers the selective advantage of silencing foreign DNA (PubMed:16763111). Binds nucleation sites in AT- rich DNA and bridges them, forming higher-order nucleoprotein complexes and condensing the chromosome (By similarity). A subset of genes are repressed by H-NS in association with Hha and/or YdgT (By similarity). SUBCELLULAR LOCATION: Cytoplasm, nucleoid. SIMILARITY: Belongs to the histone-like protein H-NS family. SIMILARITY: Belongs to the histone-like protein H-NS family.


FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 09 (Tx3-6) family.


SIMILARITY: Belongs to the NrdI family.


FUNCTION: Probable thiol-disulfide oxidoreductase that may play a role in proper chloroplast development. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the thioredoxin family. Plant CITRX-type subfamily.


FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.


FUNCTION: Acts as a regulator of Wnt signaling pathway by regulating beta-catenin (ctnnb1) nuclear localization. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FAM53 family.


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


FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. SIMILARITY: Belongs to the bacterioferritin family.


FUNCTION: Plays a role in cuticle biogenesis (PubMed:15454573, PubMed:23028364, PubMed:25480962). In complex with doxa-1 and the dual oxidase bli-3, promotes the generation of reactive oxygen species (ROS) and tyrosine cross-linking of collagen, thus stabilizing cuticular extracellular matrix (PubMed:23028364). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family.


FUNCTION: Acts as a defensive agent. Recognizes blood group fucosylated oligosaccharides including A, B, H and Lewis B-type antigens. Does not recognize Lewis A antigen and has low affinity for monovalent haptens. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the fucolectin family.


FUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-63'- linked ubiquitination of MAP3K14/NIK, leading to stabilize and activate MAP3K14/NIK. It thereby acts as an activator of the non-canonical NF- kappa-B2/NFKB2 pathway. May also play an important role in cell proliferation and/or anti-apoptosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: NAD-dependent protein deacetylase which modulates the activities of several proteins which are inactive in their acetylated form. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sirtuin family. Class III subfamily.


FUNCTION: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells (By similarity). SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV membrane protein. Nucleus envelope. Rough endoplasmic reticulum. SIMILARITY: Belongs to the nesprin family.


FUNCTION: Causes reversible depression symptom in mice when injected intracranially. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Contrapsin inhibits trypsin-like proteases. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the serpin family.


FUNCTION: Participates in nucleolar liquid-liquid phase separation (LLPS) through its N-terminal intrinsically disordered region (IDR). May be involved in ATE1-mediated N-terminal arginylation. SUBCELLULAR LOCATION: Nucleus, nucleolus Cytoplasm Note=Shuttles between the cytoplasm and nucleoplasm, a significant portion localizes to the nucleolus.


FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the SSRP1 family.


FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins (By similarity). SIMILARITY: Belongs to the KRTAP type 9 family.


FUNCTION: Baeyer-Villiger monooxygenase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer neosartorin, which exhibits antibacterial activity (PubMed:30394754, PubMed:32105084, PubMed:33891392). The two different monomeric units appear to be synthesized by the same set of enzymes, among which the Baeyer-Villiger monooxygenase nsrF is the key enzyme for the divergence of the biosynthetic routes (PubMed:32105084). The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase nsrB (PubMed:32105084). The atrochrysone carboxyl ACP thioesterase nsrC then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL (PubMed:32105084). Atrochrysone carboxylic acid is decarboxylated by the decarboxylase nsrE, and oxidized by the anthrone oxygenase nsrD to yield emodin (PubMed:32105084). Emodin is then reduced to emodin hydroquinone by the oxidoreductase nsrR (PubMed:32105084). A-ring reduction by the short chain dehydrogenase nsrJ, dehydration by the scytalone dehydratase-like protein nsrI and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol (PubMed:32105084). The Baeyer-Villiger monooxygenase nsrF accepts chrysophanol as a substrate to insert one oxygen atom at two different positions to yield the precursors of both monomric units (PubMed:30394754, PubMed:32105084, PubMed:33891392). NsrF is promiscuous/flexible in interacting with the 2 (non methylated and methylated) aromatic rings of chrysophanol, thus diverging the biosynthetic pathway at this point (PubMed:30394754, PubMed:32105084, PubMed:33891392). After the hydrolysis of the lactones, methylesterification by the methyltransferase nsrG yields respectively moniliphenone and 2,2',6'-trihydroxy-4-methyl-6-methoxya- cyldiphenylmethanone (PubMed:30394754, PubMed:32105084). The next steps are the hydroxylation by the FAD-dependent monooxygenase nsrK, followed by isomerization by the monooxygenase nsrQ (PubMed:32105084). The short chain dehydrogenase/reductase nsrO then catalyzes the C-5 ketoreduction to give the xanthone skeleton of blennolide C and 5-acetylblennolide A (PubMed:32105084). The acetyltransferase nsrL has a strict substrate specificity and uses only blennolide A but not blennolide C to yield 5- acetylblennolide A as the single-acetylated product (PubMed:30394754). In the final step of the biosynthesis, the heterodimerization of the 2 xanthones, blennolide C and 5-acetylblennolide A, is catalyzed by the cytochrome P450 monooxygenase nsrP (PubMed:30394754). NsrP can utilize at least three different xanthones as its substrates to perform the dimerization reaction (PubMed:30394754). SIMILARITY: Belongs to the AflY oxidoreductase family.


FUNCTION: Catalyzes the biosynthesis of sphingolipids with very long- chain fatty acid (VLCFA) (PubMed:31182845). Required for the formation of plasmodesmal cytoplasmic sleeve during the transition from type I to type II plasmodesmata to modulate post-sieve elements (SE) unloading and symplastic cell-to-cell molecular trafficking at the phloem pole pericycle (PPP)-endodermis interface in roots (PubMed:31182845). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sphingomyelin synthase family.


FUNCTION: Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. SIMILARITY: Belongs to the universal ribosomal protein uL10 family. SIMILARITY: Belongs to the universal ribosomal protein uL10 family.


FUNCTION: Plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis. Can stimulate cell proliferation (in vitro). May be involved in hair development. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the heparin-binding growth factors family.


FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS10 family.


SIMILARITY: Belongs to the flavin monoamine oxidase family.


FUNCTION: Highly inhibits both nicotinic acetylcholine receptors (neuronal (alpha-3/beta-4) and muscular (alpha-1/beta-1/epsilon/delta) subtypes) and the voltage-gated potassium channel Kv1.6/KCNA6 subtype. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin J superfamily.


SIMILARITY: Belongs to the UPF0265 family. SIMILARITY: Belongs to the UPF0265 family.


FUNCTION: Transmembrane reductase that may use ascorbate as an electron donor in the cytoplasm and transfer electrons across endoplasmic reticulum membranes to reduce monodehydro-L-ascorbate radical and iron cations Fe(3+) in the lumen of that compartment. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein.


FUNCTION: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low activity with 3-phenylpropionitrile (PPN). Not associated with auxin production but may be involved in cyanide detoxification. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.


FUNCTION: Loads pcna onto primed templates regulating velocity, spacing and restart activity of replication forks. May couple DNA replication to sister chromatid cohesion (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DCC1 family.


FUNCTION: Required for the activity of the plastid-encoded RNA polymerase (PEP) and full expression of genes transcribed by PEP (PubMed:24246379). Required for the proper build-up and formation of the PEP-complex (PubMed:25599833). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.


FUNCTION: Blocks olfactory (CNGA2) and retinal (CNGA1) CNG channel currents. Does not affect neither depolarization- nor caffeine-induced contraction of smooth muscle (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family.


FUNCTION: Negative regulator of flowering controlling the H4K5 acetylation levels in the FLC and FT chromatin. Positively regulates FLC expression. Component of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Component of the SWR1 complex which mediates the ATP- dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of a NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the YAF9 family.


FUNCTION: Plays a role in fertilization by controlling binding of sperm to zona pellucida and migration of spermatozoa into the oviduct probably through molecule adhesion ADAM3 (PubMed:23633567, PubMed:23969891). May play a role in signal transduction and promote protein tyrosine phosphorylation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid- anchor, GPI-anchor Membrane raft Cytoplasmic vesicle, secretory vesicle, acrosome Secreted Cytoplasmic vesicle Note=Located on plasma membrane of spermatocytes, round and elongated spermatids, and testicular spermatozoa.


FUNCTION: Strongly inhibits plasmin (Ki=0.44 nM) and trypsin (Ki=0.42 nM). Has little effect on plasma (Ki=1870 nM) and tissue (Ki=12900 nM) kallikreins. In vivo, reduces bleeding in a small animal model. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family.


FUNCTION: May be involved in the early steps of the plant defense signaling pathway. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.


FUNCTION: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the LptE lipoprotein family.


FUNCTION: Transcription termination factor that is transcriptionally active in chloroplasts. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the mTERF family.


FUNCTION: Acts as a key regulator of dendritic field orientation during development of sensory cortex. Also directs dendrites toward active axon terminals when ectopically expressed. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=Translocates from the cytosol to the nucleus in response to neuronal activity.


FUNCTION: This toxin may inhibit nicotinic acetylcholine receptor (nAChR). It has poorly reversible postsynaptic blocking activity in a chick muscle preparation and readily reversible inhibitory activity at a presynaptic site in the rat vas deferens prostatic segment most likely to prevent the release of neurotransmitters. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Boigatoxin sub-subfamily.


FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.


FUNCTION: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters (By similarity). Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the paraoxonase family.


FUNCTION: Functions in xyloglucan synthesis by adding side chains to the xylosylated glucan backbone. Involved in the galactosylation of hemicellulose xyloglucan. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 47 family.


FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.


FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal ion at the active site. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.


FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the formation of epithelial cell junctions (By similarity). Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (PubMed:36071160, PubMed:25814576, PubMed:29420470, PubMed:33734450). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the F-actin-capping protein alpha subunit family.


FUNCTION: Chemokine-binding protein that inhibits neutrophils' chemotaxis. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein G family.


FUNCTION: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature. Regulates the migration of vascular endothelial cells (By similarity). Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity). May play a role in the binding of endothelial cells to integrins (By similarity). Acts as TGF- beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:8294451). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


FUNCTION: Main toxin of bee venom with strong hemolytic activity and antimicrobial activity. It has enhancing effects on bee venom phospholipase A2 activity. This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis. It acts as a voltage-gated pore with higher selectivity for anions over cations. The ion conductance has been shown to be voltage-dependent. Self- association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids. In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response. It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore- forming activity. SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Alpha-helical peptides form toroidal pores in the prey. SIMILARITY: Belongs to the melittin family.


FUNCTION: Modulates postsynaptic dendritic arbor elaboration and synaptic maturation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the neuritin family.


FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor (PubMed:19122147). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (By similarity). Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix. Plays a key role for peroxisome movement through a direct interaction with tubulin (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peroxin-14 family.


FUNCTION: Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein (By similarity). SIMILARITY: Belongs to the UPF0122 family.


FUNCTION: This protein is essential for positively regulating the expression of transfer genes that are involved in the conjugal transfer of DNA between bacterial cells. SUBCELLULAR LOCATION: Cytoplasm.


SIMILARITY: Belongs to the herpesviridae US1 family.


FUNCTION: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria. LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin. The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation. Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. SUBCELLULAR LOCATION: Cytoplasm Synapse Note=Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1.


FUNCTION: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TBP family.


SIMILARITY: Belongs to the aldose epimerase family.


FUNCTION: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the plant LTP family.


FUNCTION: Controls floral meristem identity. Is required very early in flower development and may act here as a transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the FLO/LFY family.


FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasmic vesicle Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Toxin with unknown function in healthy organisms. On glioma cells, interacts with chloride channels (probably ClC-3/CLCN3) and MMP2 at the surface of glioma cells. This complex is then internalized via caveolae, thus inhibiting the chloride channels necessary for cell shrinkage and tumor propagation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family.


FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of a SNZ isoform. SIMILARITY: Belongs to the glutaminase PdxT/SNO family.


FUNCTION: This protein is a spindle body protein.


FUNCTION: Phosphatase which plays an essential role in the development and differentiation of the ookinete and in the formation of ookinete micronemes. SIMILARITY: Belongs to the metallophosphoesterase superfamily. SLP family.


FUNCTION: May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1- E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication. FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1- E2 complex binds to the replication origin which contains binding sites for both proteins. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the papillomaviridae E1 protein family.


FUNCTION: Antiviral effector protein expressed downstream of Sting and Rel (Relish) signaling in response to viral infection. SIMILARITY: Belongs to the C19orf12 family.


FUNCTION: Transcription activator that binds to the DNA motif 5'- CACGTGG-3' in the promoter of iron (Fe) deficiency-inducible genes as well as of genes involved in iron homeostasis, thus contributing to basal tolerance to iron deficiency, iron uptake from soil and iron transport, particularly during seed maturation and germination. Promotes the accumulation of mugineic acid family phytosiderophores (MAs). Required for ethylene-mediated signaling during iron deficiency responses. Improves growth and yield, especially in calcareous soil with low iron availability. Promotes iron concentration in shoots and grain. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bHLH protein family.


FUNCTION: DNA-binding protein that binds to both double-stranded and single-stranded DNA without significant sequence specificity to reversibly repress the transcriptional activity of chloroplast nucleoids by promoting DNA compaction and possibly regulate DNA replication. FUNCTION: Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth. SUBCELLULAR LOCATION: Plastid, chloroplast stroma, chloroplast nucleoid Plastid, chloroplast stroma Plastid stroma. SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.


FUNCTION: Folate transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter (TC 2.A.48) family.


FUNCTION: Inhibits cell growth by regulating the TOR signaling pathway upstream of the TSC1-TSC2 complex and downstream of AKT1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DDIT4 family.


FUNCTION: Plays a role in the organization of both preexisting and nascent microtubules in interphase cells. During mitosis, required for the organization and orientation of the mitotic spindle. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localized at the center of the radial microtubule array in interphase and at the spindle poles during various stages of mitosis.


FUNCTION: MFS transporter; part of the satratoxin SC3 cluster involved in the biosynthesis of satratoxins, trichothecene mycotoxins that are associated with human food poisonings (PubMed:25015739). Satratoxins are suggested to be made by products of multiple gene clusters (SC1, SC2 and SC3) that encode 21 proteins in all, including polyketide synthases, acetyltransferases, and other enzymes expected to modify the trichothecene skeleton (PubMed:25015739). SC1 encodes 10 proteins, SAT1 to SAT10 (PubMed:25015739). The largest are SAT8, which encodes a putative polyketide synthase (PKS) with a conventional non-reducing architecture, and SAT10, a putative protein containing four ankyrin repeats and thus may be involved in protein scaffolding (PubMed:25015739). The putative short-chain reductase SAT3 may assist the PKS in some capacity (PubMed:25015739). SAT6 contains a secretory lipase domain and acts probably as a trichothecene esterase (PubMed:25015739). SAT5 encodes a putative acetyltransferase, and so, with SAT6, may affect endogenous protection from toxicity (PubMed:25015739). The probable transcription factor SAT9 may regulate the expression of the SC1 cluster (PubMed:25015739). SC2 encodes proteins SAT11 to SAT16, the largest of which encodes the putative reducing PKS SAT13 (PubMed:25015739). SAT11 is a cytochrome P450 monooxygenase, while SAT14 and SAT16 are probable acetyltransferases (PubMed:25015739). The SC2 cluster may be regulated by the transcription factor SAT15 (PubMed:25015739). SC3 is a small cluster that encodes 5 proteins, SAT17 to SAT21 (PubMed:25015739). SAT21 is a putative MFS-type transporter which may have a role in exporting secondary metabolites (PubMed:25015739). The four other proteins putatively encoded in SC3 include the taurine hydroxylase-like protein SAT17, the O-methyltransferase SAT18, the acetyltransferase SAT19, and the Cys6-type zinc finger SAT20, the latter being probably involved in regulation of SC3 expression (PubMed:25015739). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway (By similarity). Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (By similarity). Plays a primary role in the maintenance of Ca(2+) homeostasis in the trans-Golgi compartment with a functional impact on Golgi and post-Golgi protein sorting as well as a structural impact on cisternae morphology. Responsible for loading the Golgi stores with Ca(2+) ions in keratinocytes, contributing to keratinocyte differentiation and epidermis integrity (By similarity). Participates in Ca(2+) and Mn(2+) ions uptake into the Golgi store of hippocampal neurons and regulates protein trafficking required for neural polarity (By similarity). May also play a role in the maintenance of Ca(2+) and Mn(2+) homeostasis and signaling in the cytosol while preventing cytotoxicity (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein Note=During neuron differentiation, shifts from juxtanuclear Golgi position to multiple Golgi structures distributed over the neural soma with a predominance in the apical dendritic trunk. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily.


FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent. FUNCTION: This peptide both inhibits the activity of the angiotensin- converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-potentiating peptide family.


FUNCTION: Part of prostatein which is the major secretory glycoprotein of ventral prostate gland. Steroid-binding protein; can bind non-polar steroids, cholesterol and a group of small proline-rich peptides (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the secretoglobin family. Lipophilin subfamily.


FUNCTION: Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FPP/GGPP synthase family.


FUNCTION: Involved in the breakdown of putrescine via hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate. SIMILARITY: Belongs to the peptidase C26 family.


FUNCTION: E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down- regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals. SUBCELLULAR LOCATION: Endomembrane system; Single-pass membrane protein Cytoplasm, cytoskeleton Cytoplasm, perinuclear region Note=Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A.


FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl- galactose ester bond in pectin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AB hydrolase superfamily. FaeA family.


FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. SUBCELLULAR LOCATION: Nucleus Cytoplasm.


FUNCTION: Methyltransferase; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (PubMed:23932525). The roles of the other FUS members are yet undetermined (PubMed:23932525). The fusarin C synthetase FUS1 is responsible for the condensation of one acetyl-coenzyme A (CoA) unit with six malonyl-CoA units and the amide linkage of the arising heptaketide and homoserine, subsequently releasing the first intermediate, prefusarin, as an alcohol with an open ring structure (PubMed:23932525). The cytochrome P450 monooxygenase FUS8 participates in multiple oxidation processes at carbon C-20 and is able to use the FUS1 product as substrate, resulting in formation of 20-hydroxy- prefusarin (PubMed:23932525). This reaction seems to be essential before the 2-pyrrolidone ring closure can be catalyzed by FUS2, generating 20-hydroxy-fusarin (PubMed:23932525). FUS8 is able to further oxidizes carbon C-20 after ring closure, resulting in the formation of carboxy-fusarin C (PubMed:23932525). As the last step, FUS9 methylates the hydroxyl group at C-21 to generate fusarin C (PubMed:23932525). Fusarin C can then rearrange to epi-fusarin C, the (z)-isomers, and fusarin A and fusarin D (PubMed:23932525). SIMILARITY: Belongs to the methyltransferase superfamily. Type-7 methyltransferase family.


FUNCTION: May modulate the activity of casein kinase-1. Inhibits CSNK1D autophosphorylation (in vitro) (By similarity). SIMILARITY: Belongs to the dysbindin family.


FUNCTION: May play a role in carbohydrates metabolism. SIMILARITY: Belongs to the phosphoglycerate mutase family.


FUNCTION: Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms (By similarity). SIMILARITY: Belongs to the hemerythrin family.


FUNCTION: Involved in pollen wall development. Catalyzes the conversion of medium-chain saturated fatty acids to the corresponding monohydroxylated fatty acids, with a preferential hydroxylation of lauric acid at the C-7 position. In-chain hydroxylated fatty acids, together with omega-hydroxylated fatty acids, are key monomeric aliphatic building blocks for sporopollenin synthesis during exine formation. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: RNA-binding protein, which probably plays a central role in gametogenesis in both males and females. Acts by binding to the 3'-UTR of mRNA, specifically recognizing GUU triplets, and promoting the translation of key transcripts (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RRM DAZ family.


FUNCTION: Has bactericidal activity. FUNCTION: Isoform 2 may play a role in the antimicrobial protection of sperm and urogenital tract epithelia. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: Dual transcriptional regulator of the TyrR regulon, which includes a number of genes coding for proteins involved in the biosynthesis or transport of the three aromatic amino acids, phenylalanine, tyrosine and tryptophan. These three aromatic amino acids act as effectors which bind to the TyrR protein to form an active regulatory protein. Acts by binding specifically to TyrR boxes in the promoter region of the target genes. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. SIMILARITY: Belongs to the nitrile hydratase subunit beta family.


FUNCTION: Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis. Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis. Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import (By similarity). Involved in the regulation of onset of chromosome condensation in the S phase (PubMed:2361953). Binds both to the nucleosomes and double-stranded DNA (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Predominantly nuclear in interphase cells. Binds to mitotic chromosomes.


FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Lipid-anchor. SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan Mic25 subfamily.


FUNCTION: Acts on leucine, isoleucine and valine. SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Transcription regulator. May recruit TATA binding protein (TBP) and possibly other basal factors to bind to the TATA box. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SPT20 family.


FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates and probably acts as a virulence factor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M36 family.


FUNCTION: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Involved in centrosome migration to the apical cell surface during early ciliogenesis. Required for ciliary structure and function, including a role in regulating length and appropriate number through modulating centrosome duplication. Required for cell branching morphology. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme.


FUNCTION: Together with SuyA, desulfonates sulfolactate to pyruvate and sulfite. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UxaA family.


FUNCTION: Major envelope protein that plays a role in the biogenesis of the viral double membrane and in egress of virus from the host cell. Produces the wrapped form of virus that is required for cell-to-cell spread. Acts as a lipase with broad specificity including phospholipase C, phospholipase A, and triacylglycerol lipase activities. SUBCELLULAR LOCATION: Virion membrane; Lipid-anchor Host Golgi apparatus, host trans-Golgi network Host endoplasmic reticulum membrane; Lipid-anchor; Cytoplasmic side Note=Component of the inner side of the enveloped virion (EV) membrane. F13 is associated post-translationally with membranes. SIMILARITY: Belongs to the orthopoxvirus OPG057 family.


FUNCTION: Histone chaperone which acts as a cofactor stimulating histone H3 acetylation by RTT109 (PubMed:21256037, PubMed:17320445, PubMed:31387991, PubMed:29300933, PubMed:19172748). Preferentially stimulates histone H3 'Lys-9' acetylation by RTT109 (PubMed:21256037, PubMed:31387991, PubMed:29300933). May also stimulate histone H3 'Lys- 56' acetylation by RTT109 (PubMed:17320445). Assembles nucleosomes (in vitro) (PubMed:19172748). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.


FUNCTION: May play a role in meristem function, and may be involved in maintaining cells in an undifferentiated, meristematic state, and its expression disappears at the same time the shoot apex undergoes the transition from vegetative to reproductive development (PubMed:11934861). Positive regulator of LATERAL ORGAN BOUNDARIES (LOB) (PubMed:11934861). Probably binds to the DNA sequence 5'-TGAC-3' (PubMed:11934861). Able to traffic from the L1 to the L2/L3 layers of the meristem, presumably through plasmodesmata (PubMed:12900451). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/KNOX homeobox family.


FUNCTION: Could be a virulence factor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase D family.


FUNCTION: Isoform large T antigen is a key early protein essential for both driving viral replication and inducing cellular transformation. Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle and by autoregulating the synthesis of viral early mRNA. Displays highly oncogenic activities by corrupting the host cellular checkpoint mechanisms that guard cell division and the transcription, replication, and repair of DNA. Participates in the modulation of cellular gene expression preceeding viral DNA replication. This step involves binding to host key cell cycle regulators retinoblastoma protein RB1/pRb and TP53. Induces the disassembly of host E2F1 transcription factors from RB1, thus promoting transcriptional activation of E2F1-regulated S-phase genes. Inhibits host TP53 binding to DNA, abrogating the ability of TP53 to stimulate gene expression. Plays the role of a TFIID-associated factor (TAF) in transcription initiation for all three RNA polymerases, by stabilizing the TBP-TFIIA complex on promoters. Initiates viral DNA replication and unwinding via interactions with the viral origin of replication. Binds two adjacent sites in the SV40 origin. The replication fork movement is facilitated by Large T antigen helicase activity. Activates the transcription of viral late mRNA, through host TBP and TFIIA stabilization. Interferes with histone deacetylation mediated by HDAC1, leading to activation of transcription. SUBCELLULAR LOCATION: Host nucleus.


FUNCTION: Probable transcription factor involved in embryogenesis and somatogenesis. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Nitric oxide-sensitive repressor of genes involved in protecting the cell against nitrosative stress. May require iron for activity.


FUNCTION: Chemotactic for neutrophils. Involved in lung-specific neutrophil trafficking during normal and inflammatory conditions. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.


FUNCTION: This potent antithrombotic agent acts in a calcium- independent manner. Exerts its anticoagulant effect by two distinct mechanisms. It binds to activated thrombin through exosite 1, blocking fibrinogen clotting, platelet activation, factor V activation and other effects, and it interacts with prothrombin (F2), decreasing its proteolytic activation -especially in the presence of factor Va. In vivo, intravenous injection before thrombosis induction causes a significant decrease in thrombus weight. Furthermore, BJC shows a prolonged effect by remaining in the plasma bound to prothrombin for at least 12 hours. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family.


FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit (By similarity). Has a role in regulating longevity, growth and brood size (PubMed:24552710). May regulate fat storage via the insulin/IGF pathway (PubMed:24552710). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.


FUNCTION: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin (PubMed:10601204, PubMed:20038185). Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S- ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S- ureidoglycolate and NH3 (PubMed:20038185). In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen (PubMed:20038185). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20 family.


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


SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Located in the cytoplasm of spermatocytes and the nuclei of round spermatids and elongated spermatids.


FUNCTION: Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MPGP family.


FUNCTION: Has antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family.


FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. SIMILARITY: Belongs to the calmodulin family.


FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME) (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the AcsF family.


FUNCTION: Necessary for the splicing of pre-mRNA. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Probable acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase. The relevance of acetyltransferase function remains unclear (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: In the C-terminal section; belongs to the acetyltransferase family. ECO subfamily. SIMILARITY: In the N-terminal section; belongs to the DNA polymerase type-Y family.


FUNCTION: Probable chaperone. SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the DnaJ family.


FUNCTION: With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity). SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS12 family.


FUNCTION: Averufin oxidase A; part of the fragmented gene cluster that mediates the biosynthesis of dothistromin (DOTH), a polyketide toxin very similar in structure to the aflatoxin precursor, versicolorin B (PubMed:12039746, PubMed:17683963, PubMed:22069571, PubMed:23207690, PubMed:23448391). The first step of the pathway is the conversion of acetate to norsolorinic acid (NOR) and requires the fatty acid synthase subunits hexA and hexB, as well as the polyketide synthase pksA (PubMed:16649078, PubMed:23207690). PksA combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor NOR (By similarity). The hexanoyl starter unit is provided to the acyl- carrier protein (ACP) domain by the fungal fatty acid synthase hexA/hexB (By similarity). The second step is the conversion of NOR to averantin (AVN) and requires the norsolorinic acid ketoreductase nor1, which catalyzes the dehydration of norsolorinic acid to form (1'S)- averantin (PubMed:23207690). The cytochrome P450 monooxygenase avnA then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN) (PubMed:23207690). The next step is performed by adhA that transforms HAVN to averufin (AVF) (PubMed:23207690). Averufin might then be converted to hydroxyversicolorone by cypX and avfA (PubMed:23207690). Hydroxyversicolorone is further converted versiconal hemiacetal acetate (VHA) by moxY (PubMed:23207690). VHA is then the substrate for the versiconal hemiacetal acetate esterase est1 to yield versiconal (VAL) (PubMed:23207690). Versicolorin B synthase vbsA then converts VAL to versicolorin B (VERB) by closing the bisfuran ring (PubMed:16649078, PubMed:23207690). Then, the activity of the versicolorin B desaturase verB leads to versicolorin A (VERA) (PubMed:23207690). DotB, a predicted chloroperoxidase, may perform epoxidation of the A-ring of VERA (PubMed:23207690). Alternatively, a cytochrome P450, such as cypX or avnA could catalyze this step (PubMed:23207690). It is also possible that another, uncharacterized, cytochrome P450 enzyme is responsible for this step (PubMed:23207690). Opening of the epoxide could potentially be achieved by the epoxide hydrolase epoA (PubMed:23207690). However, epoA seems not to be required for DOTH biosynthesis, but other epoxide hydrolases may have the ability to complement this hydrolysis (PubMed:23207690). Alternatively, opening of the epoxide ring could be achieved non-enzymatically (PubMed:23207690). The next step is the deoxygenation of ring A to yield the 5,8- dihydroxyanthraquinone which is most likely catalyzed by the NADPH dehydrogenase encoded by ver1 (PubMed:23207690). The last stages of DOTH biosynthesis are proposed to involve hydroxylation of the bisfuran (PubMed:23207690). OrdB and norB might have oxidative roles here (PubMed:23207690). An alternative possibility is that cytochrome P450 monoogenases such as avnA and cypX might perform these steps in addition to previously proposed steps (PubMed:23207690). SIMILARITY: Belongs to the avfA family.


FUNCTION: (Microbial infection) Catalyzes the phosphorylation of dZDP to dZTP, when the bacterium is infected by a phage that produces the substrate for the synthesis of dZTP (2- amino-2'-deoxyadenosine 5'- triphosphate), which is then used by the phage as a DNA polymerase substrate. FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NDK family. SIMILARITY: Belongs to the NDK family.


FUNCTION: Responsible for physiological and behavioral changes in mated female flies. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Transcriptional repressor of HOXB13 gene. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S15 family. SIMILARITY: Belongs to the peptidase S15 family.


FUNCTION: Alternative, nonproton pumping NADH:quinone oxidoreductase that delivers electrons to the respiratory chain by oxidation of NADH and reduction of quinones (PubMed:6784762, PubMed:7009604, PubMed:7020757, PubMed:6362717, PubMed:3122832, PubMed:2679883, PubMed:10664466). Utilizes NADH exclusively, and electron flow from NADH to ubiquinone does not generate an electrochemical gradient (PubMed:3122832, PubMed:2679883). FUNCTION: It may also contribute to copper homeostasis and bacterial oxidative protection (PubMed:7487066, PubMed:10510271, PubMed:16759635, PubMed:21390523). Shows cupric reductase activity, and catalyzes the reduction of Cu(2+) to Cu(+) with NADH as electron donor (PubMed:10510271). Exhibits Cu(2+) reductase activity in the presence of either FAD or quinone, but is unable to reduce Fe(3+) (PubMed:10510271). Contains thiolate-bound copper (PubMed:12176061). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Membrane-bound (PubMed:10664466). Interaction with the membrane is probably mediated by amphipathic helices and electrostatic interactions (PubMed:15581635). Copurifies with phospholipids (PubMed:7020757, PubMed:6362717). SIMILARITY: Belongs to the NADH dehydrogenase family.


FUNCTION: Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP is found in both commensal and pathogenic strains and plays a dual role in early-stage biofilm development and host cell recognition. Tip pilus adhesin, which is required for assembly of EcpA into fibers (By similarity). SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the EcpD/MatE family.


FUNCTION: Has bactericidal activity. May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility. SUBCELLULAR LOCATION: Secreted Membrane Note=Associates with tumor cell membrane-derived microvesicles. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ALG10 glucosyltransferase family.


FUNCTION: Binds to the 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL9 family.


SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4 subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cysteine-rich repeat secretory protein family.


FUNCTION: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). FUNCTION: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaA family. SIMILARITY: Belongs to the DnaA family.


FUNCTION: Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the fimbrial protein family.


FUNCTION: Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion. SIMILARITY: Belongs to the DNA polymerase type-B-like family.


FUNCTION: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'- TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities (By similarity). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the geminiviridae Rep protein family.


FUNCTION: Probable regulator of microtubule dynamics required for sperm motility (By similarity). In contrast to other members of the family, has no microtubule bundling activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell projection, cilium, flagellum Note=Present in the middle piece of sperm tail. SIMILARITY: Belongs to the TPPP family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL63 family.


FUNCTION: Probably acts as an electron carrier involved in oxygen activation and/or lignin formation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.


FUNCTION: Exports stored molybdate from the vacuole into the cytosol, making it available for molybdate cofactor (Moco) biosynthesis (PubMed:36240974). Plays a role in molybdate homeostasis as high cytosolic levels of molybdate are toxic to cells (PubMed:36240974). Not required for molybdate import into cells (PubMed:36240974). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.


FUNCTION: Transcriptional regulator that plays an important role in general stress response. SIMILARITY: Belongs to the BolA/IbaG family.


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


FUNCTION: Cargo protein of a type 1 encapsulin nanocompartment. May help nucleate Fe atoms in the interior of the encapsulin nanocompartment (Probable). Present in about 92 copies/encapsulin nanocompartment (PubMed:25024436). SUBCELLULAR LOCATION: Encapsulin nanocompartment Note=Probably lies against the interior face of the nanocompartment. SIMILARITY: Belongs to the ferritin-like superfamily.


FUNCTION: Eukaryotic-type DNA polymerase involved in viral genomic replication. DNA synthesis is protein primed, and acts in a strand displacement replication. Assembles in complex with viral pTP, DBP, host NFIA and host POU2F1/OCT1 on viral origin of replication. The polymerase covalently transfers dCMP onto pTP, thereby initiating complementary strand synthesis. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the DNA polymerase type-B family.


FUNCTION: Endonuclease that resolves Holliday junction intermediates made during homologous genetic recombination and DNA repair. Exhibits sequence and structure-selective cleavage of four-way DNA junctions, where it introduces symmetrical nicks in two strands of the same polarity at the 5' side of CC dinucleotides. Corrects the defects in genetic recombination and DNA repair associated with inactivation of RuvAB or RuvC (By similarity). SIMILARITY: Belongs to the RusA family.


FUNCTION: Virulence effector that is indispensable for endoplasmic reticulum (ER)-mediated remodeling of the Legionella pneumophila- containing vacuole (LCV) and lysosomal evasion (PubMed:33563829). Essential for intracellular replication in human monocyte-derived macrophages (hMDMs) and amoebae, as well as for intrapulmonary proliferation in mice (PubMed:33563829). SUBCELLULAR LOCATION: Secreted Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane; Single-pass membrane protein Note=Translocated into the host cell via the type IV secretion system (T4SS) (Probable). During infection, localizes to the poles of the LCV membrane (PubMed:33563829).


FUNCTION: Snake venom serine protease that induces platelet aggregation through activation of protease-activated platelet receptors (PAR1/F2R and PAR4/F2RL3). On F2R, the cleavage occurs at Arg41-Ser42 (like thrombin cleavage), and Arg46-Asn47. In normal condition of hemostasis, the cleavage of the Arg41-Ser42 bond liberates a new N-terminus that functions as an agonist. However after envenomation, the cleavage of Arg46-Asn47 bond degrades this potential agonist. This may explain why the snake protease is less potent than thrombin in causing platelet aggregation and release reaction. On F2RL3, a thrombin-like activity has also been proven by calcium release from lung fibroblasts transfected with this receptor. Possesses amidolytic activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.


FUNCTION: May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein Lysosome membrane; Peripheral membrane protein Presynaptic cell membrane; Peripheral membrane protein.


FUNCTION: Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family.


FUNCTION: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein disulfide isomerase family.


FUNCTION: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the thioredoxin family. DsbD subfamily.


FUNCTION: Hydrolyzes ester bonds of tannic acid to produce gallic acid and glucose. Exhibits no cytotoxicity in vitro in Vero cells or in vivo in a rat model. SIMILARITY: Belongs to the tannase family.


FUNCTION: Involved in cobalamin metabolism and trafficking (PubMed:18385497, PubMed:23415655, PubMed:24722857, PubMed:26364851). Plays a role in regulating the biosynthesis and the proportion of two coenzymes, methylcob(III)alamin (MeCbl) and 5'-deoxyadenosylcobalamin (AdoCbl) (PubMed:18385497, PubMed:23415655, PubMed:24722857). Promotes oxidation of cob(II)alamin bound to MMACHC (PubMed:26364851). The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR (methionine synthase) which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine (PubMed:27771510). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion.


FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mostly nuclear; oxidative stress promotes cytoplasmic localization. SIMILARITY: Belongs to the nuclear hormone receptor family. NR4 subfamily.


FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the Rho GDI family.


FUNCTION: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin family.


FUNCTION: Probable beta-1,4-glucan synthase rather involved in the synthesis of the xyloglucan backbone than cellulose. Seems to work simultaneously with xyloglucan 6-xylosyltransferase. Xyloglucan is a noncellulosic polysaccharides of plant cell wall and consists of a glucan backbone substituted by xylose, galactose and fucose (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like C subfamily.


FUNCTION: Protects cells from HOCl (hypochlorite) stress but not peroxide or diamide stress. Decreases the intracellular load of reactive oxygen species by up-regulating genes involved in methionine and cysteine biosynthesis and down-regulating Fur-regulated genes involved in iron acquisition. Has also been suggested to down-regulate expression of the flagellar regulon, decreasing motility, but this activity was not confirmed in a second study (PubMed:22223481). SIMILARITY: Belongs to the LysR transcriptional regulatory family.


FUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF- binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, but it is unclear whether it leads to the proteolytic degradation of TGF-beta proteins themselves (PubMed:18551132) or not (PubMed:14973287). By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. SUBCELLULAR LOCATION: Cell membrane Secreted Cytoplasm, cytosol Note=Predominantly secreted. Also found associated with the plasma membrane. SIMILARITY: Belongs to the peptidase S1C family.


FUNCTION: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to the vacuole (By similarity). SUBCELLULAR LOCATION: Golgi apparatus Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. SIMILARITY: Belongs to the adaptor complexes medium subunit family.


FUNCTION: May function as a riboflavin storage protein that binds and sequesters riboflavin, thereby protecting cells against undesirable reactions mediated by free riboflavin. Protects bound flavin against light damage; flavin fluorescence is rapidly quenched by interaction with Trp-39. SIMILARITY: Belongs to the dodecin family.


SIMILARITY: Belongs to the methylmalonyl-CoA epimerase family.


FUNCTION: Involved in secretion. Component of the secretory vesicle docking complex.


FUNCTION: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy. Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (By similarity). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Modulates also the pro-apoptotic function of TP53 by binding to its C- terminal transactivation domain within the nucleus and reducing its protein levels (By similarity). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (By similarity). SUBCELLULAR LOCATION: Secreted Nucleus Cytoplasm. SIMILARITY: Belongs to the S-100 family.


FUNCTION: Probable transcription factor that acts as negative regulator of trichome branching in association with HDG11 (PubMed:16778018). Seems to promote cell differentiation (PubMed:25564655). May regulate cell differentiation and proliferation during root and shoot meristem development (PubMed:25564655). Acts as positive regulator of SCL18/LAS expression (PubMed:25358340). Involved, together with PDF2, in the regulation of flower organs development by promoting the expression of APETALA 3 (AP3) in the epidermis and internal cell layers of developing flowers (PubMed:23590515). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily.


FUNCTION: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar (PubMed:16965264, PubMed:17599910, PubMed:31423530). Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-galactosamine (UDP-GalNAc) and UDP-alpha-D- glucuronate (UDP-GlcA), which are used by ER glucosyltransferases as sugar donors for the synthesis of sugar chains of glycoproteins, glycolipids and oligosaccharides (PubMed:11322953, PubMed:16965264, PubMed:17599910, PubMed:31423530, PubMed:17952091). May couple UDP- GlcNAc or UDP-GalNAc efflux to UDP-GlcA influx into the ER lumen that in turn stimulates glucuronidation and subsequent excretion of endobiotics and xenobiotics (PubMed:16965264, PubMed:17599910). Plays a role in chondroitin sulfate biosynthesis, which is important for formation of cartilage extracellular matrix and normal skeletal development (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.


FUNCTION: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Predominantly in the cytosol. SIMILARITY: Belongs to the SSU72 phosphatase family.


FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1- carboxylate (SHCHC) to 2-succinylbenzoate (OSB). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. MenC type 1 subfamily.


FUNCTION: Encapsidates the viral genome into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. Plays a role in protection of the genome from degradation, virus acquisition and transmission by insect vectors, infectivity, and systemic movement. The CP of monopartite geminiviruses is absolutely essential for virus movement (By similarity). SUBCELLULAR LOCATION: Virion Host nucleus Note=It is actively transported into the host cell nucleus. It may be exported out of the nucleus through a nuclear export signal for cell- to-cell movement and spread (By similarity). SIMILARITY: Belongs to the geminiviridae capsid protein family.


FUNCTION: Catalyzes the dehydrogenation at the alpha-beta position of ACP-bound acyl chains. This results in the introduction of a double bond in the lipidic chain, which is further transferred to the epsilon- amino group of lysine residue in the mycobactin core by MbtK (By similarity). SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.


FUNCTION: NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles. SUBCELLULAR LOCATION: Virion Note=Localizes to the virion core. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.


FUNCTION: Strongly inhibits the collagen-induced human platelet aggregation. Hydrolyzes the Aalpha-chain of fibrinogen (FGA), without cleavage of Bbeta- and gamma-chains. Induces apoptosis and strongly inhibits proliferation of endothelial cells as well as adhesion of the cells to extracellular matrix proteins (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIc sub-subfamily.


SIMILARITY: Belongs to the peptidase C56 family.


FUNCTION: Involved in the heme and chlorophyll biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase family.


FUNCTION: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume, membrane potential stabilization, signal transduction and transepithelial transport (By similarity). Involved in the regulation of aldosterone production. The opening of CLCN2 channels at hyperpolarized membrane potentials in the glomerulosa causes cell membrane depolarization, activation of voltage-gated Ca2+ channels and increased expression of aldosterone synthase, the rate-limiting enzyme for aldosterone biosynthesis (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC- 2/CLCN2 subfamily.


FUNCTION: Cell surface proteoglycan (By similarity). Negatively regulates the hedgehog signaling pathway (By similarity). Positively regulates the canonical and non-canonical Wnt signaling pathways (By similarity). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (By similarity). Inhibits the dipeptidyl peptidase activity of DPP4 (By similarity). Plays a role in limb patterning and skeletal development (By similarity). Modulates the effects of growth factors on renal branching morphogenesis (By similarity). Required for coronary vascular development (By similarity). Plays a role in regulating cell movements during gastrulation (PubMed:14610063). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. SIMILARITY: Belongs to the glypican family.


FUNCTION: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin B subfamily.


FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus. Isoform gamma may have a role in patterning and cellular proliferation of skeletal elements in the precartilaginous/cartilaginous skeleton. SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm. Note=Locates to the areas within the cytoplasm. SUBCELLULAR LOCATION: [Isoform Alpha]: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm. Note=Locates to the areas within the cytoplasm. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Receptor class 7 subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase C40 family.


FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites. DSIF can also positively regulate transcriptional elongation and is required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. DSIF acts to suppress transcriptional pausing in transcripts derived from the HIV-1 LTR and blocks premature release of HIV-1 transcripts at terminator sequences. FUNCTION: Component of the DRB sensitivity-inducing factor complex (DSIF complex), which regulates mRNA processing and transcription elongation by RNA polymerase II. DSIF positively regulates mRNA capping by stimulating the mRNA guanylyltransferase activity of RNGTT/CAP1A. DSIF also acts cooperatively with the negative elongation factor complex (NELF complex) to enhance transcriptional pausing at sites proximal to the promoter. Transcriptional pausing may facilitate the assembly of an elongation competent RNA polymerase II complex. DSIF and NELF promote pausing by inhibition of the transcription elongation factor TFIIS/S-II. TFIIS/S-II binds to RNA polymerase II at transcription pause sites and stimulates the weak intrinsic nuclease activity of the enzyme. Cleavage of blocked transcripts by RNA polymerase II promotes the resumption of transcription from the new 3' terminus and may allow repeated attempts at transcription through natural pause sites (By similarity). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SPT4 family.


FUNCTION: Aldose reductase with a broad substrate specificity. Reduces the cytotoxic compound methylglyoxal (MG) to acetol and (R)- lactaldehyde under stress conditions. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation (PubMed:11525399). In pentose-fermenting yeasts, aldose reductase catalyzes the reduction of xylose into xylitol. The purified enzyme catalyzes this reaction, but the inability of S.cerevisiae to grow on xylose as sole carbon source indicates that the physiological function is more likely methylglyoxal reduction (Probable) (PubMed:11722921). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the aldo/keto reductase family.


FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Seems also to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs and acting as a nidus for in situ immune complex formation. FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Seems also to act as a fortuitous virulence factor in delayed sequelae by binding to heparan sulfate-proteoglycans in the extracellular matrix of target organs and acting as a nidus for in situ immune complex formation (By similarity). SIMILARITY: Belongs to the bacterial histone-like protein family.


FUNCTION: Serine protease inhibitor that inhibits both tissue and plasma kallikreins. Has hemolytic activity. Inhibits voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily.


FUNCTION: Binds to acetylcholine. Modulates neuronal synaptic transmission. SUBCELLULAR LOCATION: Synaptic cleft Note=Released in an acetylcholine-dependent manner in the synaptic cleft. SIMILARITY: To the extracellular portion of ligand-gated ionic channels family.


FUNCTION: Acts as a positive activator of the GCN2 protein kinase activity in response to in response to low amino acid, carbon, or purine availability (PubMed:7621831, PubMed:10733573). Component of the GCN1-GCN20 complex that forms a complex with GCN2 on translating ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone to facilitate delivery of uncharged tRNAs that enter the A site of ribosomes to the tRNA-binding domain of GCN2, and hence stimulating GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:10775272, PubMed:15722345). Participates in gene-specific mRNA translation activation, such as the transcriptional activator GCN4, by promoting the GCN2-mediated phosphorylation of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4- mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:15722345). SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.


FUNCTION: Highly glycosylated atypical beta-defensin involved in several aspects of sperm function. Facilitates sperm transport in the female reproductive tract and contributes to sperm protection against immunodetection; both functions are probably implicating the negative surface charge provided by its O-linked oligosaccharides in the sperm glycocalyx. Involved in binding of sperm to oviductal epithelial cells to form a sperm reservoir until ovulation. Release from the sperm surface during capacitation and ovaluation by an elevation of oviductal fluid pH is unmasking other surface components and allows sperm to penetrate the cumulus matrix and bind to the zona pellucida of the oocyte. In vitro has antimicrobial activity and may inhibit LPS- mediated inflammation (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted by epididymal cells and is absorbed to the surface of sperm during transit through the epididymis. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: Peptide which plays a role in the humoral immune response to a subset of filamentous fungi, including F.oxysporum and F.verticillioides. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C56 family. HchA subfamily.


FUNCTION: Probable serine protease. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Golgi apparatus, cis-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase S54 family.


FUNCTION: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors. Phosphorylates the CTD (C- terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.


FUNCTION: Versicolorin B desaturase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins (PubMed:15094053, PubMed:8368837, PubMed:15006741). The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) (PubMed:15006741). Within the aflatoxin pathway, the versicolorin B desaturase aflL catalyzes the conversion of versicolorin B (VERB) to versicolorin A (VERA) (PubMed:8368837, PubMed:15006741). The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'- hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'- oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O- methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 (PubMed:15006741). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.