FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. SIMILARITY: Belongs to the alanine racemase family.


FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily.


FUNCTION: Binds long-chain acyl-coenzyme A molecules with a strong preference for unsaturated C18:1-CoA, lower affinity for unsaturated C20:4-CoA, and very weak affinity for saturated C16:0-CoA. Does not bind fatty acids. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Has antibacterial activity against the Gram-positive bacteria L.monocytogenes, L.lactis subsp lactis and L.curvatus H28, but not against the Gram-positive bacteria L.curvatus CWBI-B28, L.brevis and L.plantarum or the Gram-negative bacteria E.coli and Pseudomonas sp 55. Has no antifungal activity against S.cerevisiae, Penicillium sp BKS- TAN2 or A.niger. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. SUBCELLULAR LOCATION: Periplasm Note=Is attached to the inner membrane when interacting with the MsrQ subunit. SIMILARITY: Belongs to the MsrP family.


FUNCTION: Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, a precursor for Pseudomonas quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which is required to induce the genes for the biosynthesis of the virulence factor pyocyanine (PCN), a characteristic blue-green phenazine pigment produced by P.aeruginosa (PubMed:11591691, PubMed:2153661, PubMed:23449919). In the first step, the glutamine-binding beta subunit (PhnB) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (PhnA) to produce anthranilate (By similarity). SIMILARITY: Belongs to the anthranilate synthase component I family.


FUNCTION: Provides adhesiveness to the mussel's foot. Mussels produce one of the strongest water insoluble glues. The mussel's adhesive is a bundle of threads, called a byssus, formed by a fibrous collagenous core coated with adhesive proteins (By similarity). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Mainly localizes to Golgi apparatus. SIMILARITY: Belongs to the PGAP3 family.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL3 subfamily.


FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family. Protoheme IX farnesyltransferase subfamily.


FUNCTION: Specificity, limited to carboxyl side of arginine residue in B-chain of insulin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Ligand-dependent transcription factor probably involved in the retinoic acid response pathway. Binds 9-cis-retinoic acid (By similarity). Involved in embryo development, in particular eye and shell formation. May play a role in growth cone steering. SUBCELLULAR LOCATION: Cytoplasm Nucleus Membrane; Peripheral membrane protein Cell projection, axon Cell projection, growth cone Note=Not present in nucleus of neurons in adult CNS. Detected in neurites and growth cones of cultured neurons. SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 subfamily.


FUNCTION: Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the UPF0400 (RTT103) family.


FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. May play a role in accumulation of expanded polyglutamine (polyQ) protein huntingtin (HTT) (By similarity). SUBCELLULAR LOCATION: Nucleus Note=In the nucleus, associates with a subnuclear dot-like structure.


FUNCTION: Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).


FUNCTION: Could be part of an ABC transporter complex. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MlaE permease family.


FUNCTION: May be part of a complex that binds ubiquitinated proteins and that is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. SIMILARITY: Belongs to the NPL4 family.


FUNCTION: Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.


FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine. May be involved in virulence (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M35 family.


FUNCTION: Modulates the activity of the EnvZ/OmpR two-component regulatory system, probably by directly modulating EnvZ enzymatic activity and increasing stability of phosphorylated OmpR. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MzrA family.


SIMILARITY: Belongs to the UPF0148 family.


FUNCTION: Part of the ABC transporter complex PotFGHI involved in putrescine uptake (PubMed:8416922, PubMed:23719730). Responsible for the translocation of the substrate across the membrane (Probable). Imports putrescine for maintenance of the optimal concentration of polyamines necessary for cell growth in the presence of glucose (PubMed:23719730). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.


FUNCTION: Part of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PIGH family.


FUNCTION: Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (PubMed:27918543). The side chain of Glu-231 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (PubMed:27918543). Acts as a key regulator of the ERN1/IRE1-mediated unfolded protein response (UPR) by mediating AMPylation or de-AMPylation of HSPA5/BiP (PubMed:27918543). In unstressed cells, acts as an adenylyltransferase by mediating AMPylation of HSPA5/BiP at 'Thr-518', thereby inactivating it (PubMed:26673894, PubMed:29064368, PubMed:27918543). In response to endoplasmic reticulum stress, acts as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from HSPA5/BiP at 'Thr-518', leading to restore HSPA5/BiP activity (PubMed:27918543). Although it is able to AMPylate RhoA, Rac and Cdc42 Rho GTPases in vitro, Rho GTPases do not constitute physiological substrates (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the fic family.


SIMILARITY: Belongs to the universal ribosomal protein uL4 family.


FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family.


FUNCTION: Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells. SIMILARITY: Belongs to the SAPAP family.


FUNCTION: Hydroxylase/desaturase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host- selective toxin (PubMed:29844193). The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction with oxygen molecules (PubMed:11701851). These reactive oxygen species cause damage to various cellular components including lipids, proteins and nucleic acids (PubMed:11701851). The first step of cercosporin biosynthesis is performed by the polyketide synthase CTB1 which catalyzes the formation of nor-toralactone (Probable). The starter unit acyltransferase (SAT) domain of CTB1 initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain. The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (Probable). The bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (Probable). The O-methyltransferase CTB2 further methylates the nascent OH-6 of the CBT3 product, blocking further oxidation at this site before the reductase CTB6 reduces the 2-oxopropyl ketone at position C7, giving naphthalene (Probable). The FAD-dependent monooxygenase CTB5 in concert with the multicopper oxidase CTB12 are responsible for homodimerization of naphthalene with CTB7 installing the dioxepine moiety, finally producing cercosporin (Probable). The fasciclin domain- containing protein CTB11 might act with CTB5 and CTB12 whereas the roles of CTB9 and CTB10 have still to be elucidated (By similarity). SIMILARITY: Belongs to the asaB hydroxylase/desaturase family.


FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:18983167). May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development (PubMed:18983167). Binding to RAF1 reduces RAF1 'Ser-259' inhibitory- phosphorylation and stimulates RAF1-dependent EGF-activated ERK- signaling (PubMed:23509299). Protects against cell death induced by hydrogen peroxide and staurosporine (PubMed:23509299). SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE8 subfamily.


FUNCTION: Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of APP. Inhibits APP transport to the cell surface and further shedding. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the TMEM59 family.


SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.


FUNCTION: Required for the synthesis of amylose in endosperm. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. Note=Amyloplast or chloroplast, granule-bound. SIMILARITY: Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.


FUNCTION: Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone (By similarity). SUBCELLULAR LOCATION: Mitochondrion.


FUNCTION: Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis (PubMed:14990792, PubMed:16751398). Inhibits osteoclast formation (PubMed:11278931, PubMed:12374791). Binds high molecular weight sulfated glycosaminoglycans (PubMed:15123656). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.


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


FUNCTION: Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA. SIMILARITY: Belongs to the helicase family. PriA subfamily.


FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. May preferentially transfer long chains during branching. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid, amyloplast. SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.


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


FUNCTION: Eca and bai are essential, though not redundant, for dorsoventral patterning of the embryo. Specifically required during early embryogenesis for the activity of maternal tkv, while the zygotic tkv is not affected (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMP24/GP25L family.


FUNCTION: Catalyzes the incorporation of an ammonium ion into alpha- ketoglutarate to form L-glutamate, the major route of assimilation of ammonia into an organic form in yeast. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.


FUNCTION: Scavenger receptor that displays several functions associated with host defense. Promotes binding and phagocytosis of Gram-positive, Gram-negative bacteria and yeast. Mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. Binds to several carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent manner and internalizes specifically GalNAc in nurse-like cells. Binds also to sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May also play a role in the clearance of amyloid-beta in Alzheimer disease. SUBCELLULAR LOCATION: Membrane; Single- pass type II membrane protein Note=Forms clusters on the cell surface.


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


FUNCTION: Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L- carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA. FUNCTION: Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L- carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CoA-transferase III family. CaiB subfamily.


FUNCTION: Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. The dissociation is voltage- dependent. This toxin is active on insects. It is also highly toxic to crustaceans and has a measurable but low toxicity to mice. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily.


FUNCTION: Has a crucial role in virus assembly and budding. The matrix interacts with the RNP complex and this association serves two functions: facilitate virion assembly and inhibit the viral transcriptase activity. Early in infection, M is localized to the nucleus and may inhibit host cell transcription. Later on, M can associate with lipid rafts supposely by interacting with the cytoskeleton and with the cytoplasmic tail of glycoprotein G. The binding of M to host membrane is stabilized by the surface expression of the viral glycoproteins. These interactions may allow virus formation by mediating association of the nucleocapsid with the nascent envelope (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm Host nucleus Host cell membrane; Peripheral membrane protein; Cytoplasmic side Note=During bud formation, associates at the inner side of the plasma membrane of infected cells. SIMILARITY: Belongs to the paramyxoviruses M protein family.


FUNCTION: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells. May play a crucial role in the control of de- differentiation and cell proliferation processes required for lateral root formation. Is essential for embryo development. Is involved in the geminivirus mungbean yellow mosaic virus (MYMV) DNA replication, presumably in conjunction with other host factors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MCM family.


SIMILARITY: To E.coli YfcO.


FUNCTION: Exerts antifungal activity through its carbohydrate-binding specificity.


FUNCTION: Low-spin monoheme cytochrome c.


FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4- aminobutanal. Also functions as a cadaverine transaminase in a a L- lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily.


FUNCTION: Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD). Targets the misfolded LRR receptor kinase BRI1. Functions redundantly with HRD3B. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HRD1 family.


FUNCTION: Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (PubMed:20215400). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (PubMed:20215400). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (By similarity). Involved in memory-related synaptic plasticity in the hippocampus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, dendrite Cytoplasm, cell cortex Cell junction Cell projection, growth cone Note=In the absence of antigen, evenly distributed throughout subcortical regions of the T-cell membrane and cytoplasm (PubMed:20215400). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation clusters (SMAC) (PubMed:20215400). Colocalized with RUFY3 and F-actin at the transitional domain of the axonal growth cone (By similarity).


FUNCTION: Essential for the proper assembly of the glomerular and tubular basement membranes in kidney. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tetraspanin (TM4SF) family.


FUNCTION: Has no ubiquitin ligase activity on its own. The heterodimer with UBC catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. May play a role in the control of progress through the cell cycle and differentiation. May play a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Acts as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates (in vitro). SIMILARITY: Belongs to the RING-type zinc finger family. LOG2 subfamily.


FUNCTION: Probably part of an ABC transporter complex involved in host cell binding either through secretion of an adherence factor or through maintaining the architecture and integrity of the mycobacterial cell envelope (PubMed:17030567). Could be required for host endothelial-cell invasion and/or intracellular survival (PubMed:16586367). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC-4 integral membrane protein family.


FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade 'B2' sub-subfamily.


FUNCTION: Exhibits phosphatidate phosphatase (PAP) activity in vitro. May play a primary role as PAP in plastids. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family.


FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. Note=Inner surface of plasma membrane. SIMILARITY: Belongs to the small GTPase superfamily. Ras family.


FUNCTION: Enhances virion budding, by targeting human CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its receptor human CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to interfere with the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo (By similarity). SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the HIV-1 VPU protein family.


FUNCTION: Putative toxin component of a putative type VII toxin- antitoxin (TA) system. Its cognate antitoxin might be MJ0604. SIMILARITY: Belongs to the UPF0332 family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: In the central section; belongs to the complex I 30 kDa subunit family. SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa subunit family. SIMILARITY: In the N-terminal section; belongs to the complex I 20 kDa subunit family.


FUNCTION: [p6-gag]: Plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1. FUNCTION: [Nucleocapsid protein p7]: Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. As part of the polyprotein, participates in gRNA dimerization, packaging, tRNA incorporation and virion assembly. FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). FUNCTION: [Matrix protein p17]: Targets the polyprotein to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus (By similarity). Matrix protein is part of the pre-integration complex. Implicated in the release from host cell mediated by Vpu. Binds to RNA (By similarity). FUNCTION: [Capsid protein p24]: Forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion (By similarity). Most core are conical, with only 7% tubular (By similarity). The core is constituted by capsid protein hexamer subunits (By similarity). The core is disassembled soon after virion entry (By similarity). Host restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral capsids and cause premature capsid disassembly, leading to blocks in reverse transcription (By similarity). Capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity). Host PIN1 apparently facilitates the virion uncoating (By similarity). On the other hand, interactions with PDZD8 or CYPA stabilize the capsid (By similarity). The capsid interacts with high affinity with human NONO, promoting detection of viral DNA by CGAS, leading to CGAS-mediated inmmune activation (By similarity). SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion. SUBCELLULAR LOCATION: [Capsid protein p24]: Virion. SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane; Lipid-anchor Host nucleus Host cytoplasm. SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane; Lipid-anchor Host endosome, host multivesicular body Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. SIMILARITY: Belongs to the primate lentivirus group gag polyprotein family.


FUNCTION: Secreted protein which suppresses the host allergic response by inhibiting the interaction of host IL33 with its receptor in order to maintain parasitic infection (PubMed:29045903). Binds to both host IL33 and host nuclear DNA and this dual binding blocks the interaction of IL33 with its receptor, and tethers IL33 within necrotic cells, preventing its release, and blocking allergic response initiation (PubMed:29045903). SUBCELLULAR LOCATION: Secreted Host nucleus.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS13 family.


FUNCTION: Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the proteasome inhibitor PI31 family.


FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (PubMed:20018874). Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the Wnt family.


FUNCTION: Degrades exclusively diarylether compounds having carboxyl groups in the 3- or 4-position. Yields a hemiacetal that spontaneously hydrolyzes to phenol and protocatechuate. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family.


FUNCTION: This transforming protein appears to have a protein-kinase activity. SUBCELLULAR LOCATION: Host cytoplasm.


FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs (By similarity). Contributes to long-term survival under nutrient deprivation, to stationary phase-dependent hydrogen peroxide and acid stress resistance and is required for prolonged survival in the intracellular environment of the host macrophage. Therefore, contributes not only to a generalized stress response in stationary phase but also to pathogenesis in mice, allowing the brucellae to adapt to the harsh conditions encountered within macrophages. FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. SIMILARITY: Belongs to the Hfq family.


FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Elongation factor component of the little elongation complex (LEC), a complex required to regulate small nuclear RNA (snRNA) gene transcription by RNA polymerase II and III (PubMed:22195968, PubMed:23932780). Specifically required for stimulating the elongation step of RNA polymerase II- and III-dependent snRNA gene transcription (PubMed:23932780). ELL also plays an early role before its assembly into in the SEC complex by stabilizing RNA polymerase II recruitment/initiation and entry into the pause site. Required to stabilize the pre-initiation complex and early elongation. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Nucleus, Cajal body Note=Colocalizes with EAF2 to nuclear speckles (PubMed:12446457). Colocalizes with coilin in subnuclear cajal and histone locus bodies (PubMed:12686606). Translocates in the LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1- dependent manner. Associates to transcriptionally active chromatin at snRNA genes(PubMed:23932780). SIMILARITY: Belongs to the ELL/occludin family.


FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.


FUNCTION: Small GTPase-like component of the intraflagellar transport (IFT) complex B required for both anterograde and retrograde intraflagellar transport. May be involved in cargo loading of the retrograde transport. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbY family.


FUNCTION: Plays a role in pre-mRNA splicing by regulating the release and transfer of U4/U6.U5 tri-small nuclear ribonucleoprotein (tri- snRNP) complexes from their assembly site in Cajal bodies to nuclear speckles, thereby contributing to the assembly of the pre-catalytic spliceosome on target pre-mRNAs (PubMed:34023904). May also participate in recycling of snRNPs back to Cajal bodies during splicing (PubMed:34023904). Plays a role in regulating MAGI2-mediated endocytosis (PubMed:24608321). Anchoring/scaffolding protein that is a part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal development and maintenance of cochlear hair cell bundles. Required for normal hearing. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein Cell projection, cilium Nucleus speckle Nucleus, Cajal body Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Photoreceptor inner segment Note=Detected at the tip of cochlear hair cell stereocilia. Recruited to the cell membrane via interaction with CDH23 or PCDH15 (By similarity). In photoreceptor cilia, detected predominantly at the cilium base (By similarity). Expressed in the pericentriolar region of the centrosome (By similarity).


FUNCTION: Involved in copper transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.


FUNCTION: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3. The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration. Involved in platelet activation. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Single-pass type I membrane protein Note=Localized at tight junctions of both epithelial and endothelial cells. SIMILARITY: Belongs to the immunoglobulin superfamily.


FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner. FUNCTION: Catalyzes the first step of the '4S' desulfurization pathway that removes covalently bound sulfur from dibenzothiophene (DBT) without breaking carbon-carbon bonds. Sulfur dioxygenase which converts DBT to DBT-sulfone (DBTO2 or DBT 5,5-dioxide) in a stepwise manner. In (PubMed:7961424) DBTO (dibenzothiophene-5-oxide) was reported not to be a substrate, in (PubMed:7574582, PubMed:9634856, PubMed:8824615, PubMed:9308179) it is reported to be a substrate (PubMed:7961424, PubMed:7574582, PubMed:9634856, PubMed:8824615, PubMed:9308179). Can also use benzyl sulfide and benzyl sulfoxide as substrates, although benzyl sulfoxide is a poor substrate (PubMed:8824615). The pathway substrate specificity has been augmented using mutagenesis, however no mutations allowed use of alkylated thiophenes (PubMed:11823208). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DszC flavin monooxygenase family.


FUNCTION: Inner envelope protein involved, through its interaction with host dynein, in the intracellular microtubule-dependent transport of viral capsid toward viral factories (By similarity). Seems to induce caspase-3 activation and apoptosis (By similarity). Plays a role in virion morphogenesis by recruiting and transforming the host ER membranes into the precursors of the viral envelope (By similarity). Involved in virus attachment to the host cell (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Host cytoplasm, host cytoskeleton Host endoplasmic reticulum membrane Note=Localizes to the viral factory at 16 hpi. Host DYNLL1 and viral p54 interact at the microtubular organizing center (By similarity). Found in the inner envelope of the virus (By similarity). SIMILARITY: Belongs to the asfivirus envelope protein p54 family.


FUNCTION: Probably involved in the organization of the actin cytoskeleton. Induced membrane extensions in fibroblasts (By similarity). SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the BORG/CEP family.


FUNCTION: Probable transcriptional regulator involved in the regulation of the proneural AS-C genes and the neurogenic genes of the enhancer of split complex. Could specifically activate proneural genes in the ventral-most neuroectoderm. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NK-2 homeobox family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 75 kDa subunit family.


FUNCTION: May regulate the kinase DMPK. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes to nuclear foci. SIMILARITY: Belongs to the small heat shock protein (HSP20) family.


SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Chromosome, centromere Note=Predominantly expressed in nucleolus. In mitosis associated with centromeres and concentrated at the midbody in cytokinesis (By similarity). SIMILARITY: Belongs to the NOA36 family.


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


FUNCTION: Catalyzes the oxidation of D-2-hydroxyglutarate to alpha- ketoglutarate. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type 4 family.


FUNCTION: Associated with the oxygen-evolving complex of photosystem II. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane. Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the psbR family.


FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in sucrose transport. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.


FUNCTION: May be a modulator of the apoptotic response through its ability to affect mitochondrial stability (By similarity). Adapter protein involved in tyrosine kinase and CD28 signaling. Seems to affect CD28-mediated activation of the RE/AP element of the interleukin-2 promoter. SUBCELLULAR LOCATION: Cytoplasm. Nucleus.


FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate.


FUNCTION: Plays a major role in single RNA editing events in chloroplasts. Acts as a site-recognition transacting factor involved in the edition of the unique site (corresponding to cytidine-488) of rpoC1, which is a plastid-encoded subunit of the chloroplast DNA- directed RNA polymerase. May provide the catalytic activity for editing site conversion (PubMed:24194514). Involved in leaf vasculature patterning (PubMed:18643975). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the PPR family. PCMP-H subfamily.


FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Mediated by glycine. This protein plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. It mediates neuronal functions in glutamate neurotransmission. Is involved in the cell surface targeting of NMDA receptors. Plays a role in associative learning and in long-term memory consolidation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane Postsynaptic density. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family.


FUNCTION: Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the selectin/LECAM family.


FUNCTION: Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes. SUBCELLULAR LOCATION: Late endosome membrane Lysosome membrane Cytoplasmic vesicle, phagosome membrane Note=Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes.


FUNCTION: Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Note=Vacuolar and perivacuolar punctate structures. SIMILARITY: Belongs to the WD repeat PROPPIN family.


SIMILARITY: Belongs to the ycf51 family.


FUNCTION: Secreted effector that contributes strongly to virulence during infection by P.capsici. Causes large necrotic areas in both host C.annuum and non-host N.benthamiana. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Necrosis inducing protein (NPP1) family.


FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Required for the correct development of pollen. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the peptidase C19 family.


FUNCTION: 3'-5' exonuclease that preferentially uses ssDNA as substrate. Plays a role in group I intron homing. May play a role in the final step of host DNA degradation, by scavenging DNA into mononucleotides.


FUNCTION: Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis (PubMed:9044836, PubMed:15073321, PubMed:16652156, PubMed:17159900, PubMed:17289572). Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway (PubMed:8985253). SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Putative ATP-binding protein, and an energy-coupling component of capsule polysaccharide export apparatus. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: Dual methyltransferase. It catalyzes N-terminal methylation of target proteins via its C-terminus. It catalyzes dimethylation on lysine residues of target proteins via its N-terminus. SIMILARITY: Belongs to the methyltransferase superfamily.


FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatE shares overlapping functions with TatA. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TatA/E family. TatE subfamily.


FUNCTION: Acts as a metalloprotease. Penetrates intact tissue and specifically cleaves the vesicle-associated membrane protein 2 (VAMP2) (part of the SNARE complex) involved in pancreatic secretion, thus disrupting the normal vesicular traffic (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family.


FUNCTION: An RNase that has endonuclease and 5'-3' exonuclease activity. The 5'-exonuclease activity acts on 5'-monophosphate but not 5'-triphosphate ends. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Plays the major role in pre-23S rRNA maturation, and a minor role in processing of pre- 5S and pre-16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. Bacterial RNase J subfamily.


FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family.


FUNCTION: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase superfamily. PEMT/PEM2 methyltransferase family.


FUNCTION: Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (PubMed:17275818, PubMed:18667693). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (PubMed:18667693). SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Cytoplasm, perinuclear region Cell projection, growth cone. SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase family.


FUNCTION: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). 2-O-sulfation within HS, particularly of iduronate residues, is essential for HS to participate in a variety of high-affinity ligand- binding interactions and signaling processes. Required for metanephric development of kidney formation, suggesting that 2-O-sulfation within HS is essential for signaling between ureteric bud and metanephric mesenchyme. Mediates 2-O-sulfation of both L-iduronyl and D-glucuronyl residues. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 3 family.


FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells (PubMed:1550672). Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:1550672). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:20202934). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes (PubMed:9305895). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells (PubMed:1550672, PubMed:20202934). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Perikaryon Cell projection, dendrite Note=Localized uniformly throughout cell bodies and dendrites (PubMed:10719893). Colocalizes with KCNB1 to high- density somatodendritic clusters on cortical pyramidal neurons (PubMed:20202934). SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.2/KCNB2 sub-subfamily.


FUNCTION: Involved in cellular response to chemical stress and may contribute to resistance toward antimicrobial natural compounds as well as drugs. Catalyzes the methylation and detoxification of the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2- heptyl-1-methoxy-4(1H)-quinolinone (HMOQ). FUNCTION: Involved in cellular response to chemical stress and may contribute to resistance toward antimicrobial natural compounds as well as drugs (Probable). Catalyzes the methylation and detoxification of the P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2-heptyl-1-methoxy-4(1H)-quinolinone (HMOQ) (PubMed:33064871). Can also methylate 3-bromo-2-heptyl-1-hydroxy-4(1H)-quinolinone, and shows much lower activity with 1-hydroxyquinolin-4(1H)-one, quercetin, 4- hydroxyquinolin-2(1H)-one (DHQ) and 4-hydroxyisoquinolin-1(2H)-one (PubMed:33064871). In addition, N-methylates and abolishes the mycobactericidal activity of 3-methyl-1-oxo-2-[3-oxo-3-(pyrrolidin-1- yl)propyl]-1,5-dihydrobenzo[4,5]imidazo[1,2-a]pyridine-4-carbonitrile (compound 14), an inhibitor of DprE1 (PubMed:27432954). Also methylates and reduces the inhibitory effect of TPSA (2-[5-(2-{[4-(2-thienyl)-2- pyrimidinyl]sulfanyl}acetyl)-2-thienyl]acetic acid), an inhibitor of GlmU acetyltransferase (PubMed:31380295). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily.


FUNCTION: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L- serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine. FUNCTION: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L- serine to L-serine (PubMed:12213811, PubMed:15291819, PubMed:9222972, PubMed:14673469, PubMed:25080166). L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator (PubMed:14673469). May also act on O-phospho-D-serine (Probable). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.


SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the glycosyltransferase 34 family.


FUNCTION: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity. Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing the charging of Ser adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent peptides. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SWP1 family.


SIMILARITY: Belongs to the UPF0440 family.


FUNCTION: Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids.


FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. It is not essential for viral replication and recombination. SIMILARITY: Belongs to the ATP-dependent DNA ligase family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the phospholipid scramblase family.


FUNCTION: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.


FUNCTION: Secreted effector that acts as an elicitor that induces cell death in host plant cells. SUBCELLULAR LOCATION: Secreted Host nucleus. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.


FUNCTION: Responsible for EBV binding to the CR2 receptor on human B- cells. FUNCTION: Initiates virion attachment to host B-lymphocyte cell, leading to virus entry. Acts by binding to host CR2 at the surface of B-lymphocytes, facilitating the binding of viral glycoprotein gp42 to HLA class II molecules. Attachment triggers virion-host membrane fusion and invasion of the host cell (By similarity). SUBCELLULAR LOCATION: Virion membrane. Note=Most abundant component of the viral envelope. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. Host membrane; Single-pass membrane protein. Note=Most abundant component of the viral envelope. SIMILARITY: Belongs to the Epstein-Barr GP350 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.


FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Plays an important role in the correct PLK1 localization to the mitotic kinetochores. A scaffold protein responsible for the initial recruitment and maintenance of the kinetochore PLK1 population until its degradation. Involved in transcriptional repression (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, centromere, kinetochore Note=Localizes in the kinetochore domain of centromeres. Colocalizes with PLK1 at the interzone between the inner and the outer kinetochore plates (By similarity). SIMILARITY: Belongs to the CENP-U/AME1 family.


FUNCTION: Oxidizes mannitol to mannose. Provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level (By similarity). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the DVL/RTFL small polypeptides family.


FUNCTION: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate (PubMed:15213226, PubMed:18162462, PubMed:18245280, PubMed:2361939, PubMed:9150242). It can also use succinate as acceptor (PubMed:18245280, PubMed:2361939). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CoA-transferase III family. Frc subfamily.


FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in mitomycin-C (MMC)-induced DNA repair: acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCL and FANCI. May contribute to ubiquitination and degradation of BRCA1. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination. SUBCELLULAR LOCATION: Nucleus Note=Accumulates to chromatin. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Hyaluronidase that mediates hydrolysis of (1->3)-linkages between beta-D-glucuronate and N-acetyl-D-glucosamine residues in hyaluronate. Very specific to hyaluronate: not able to hydrolyze chitin, heparin or chondroitin sulfate. SIMILARITY: Belongs to the glycosyl hydrolase 79 family.


FUNCTION: Probable DNA-binding regulatory protein involved in cell-fate specification. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CUT homeobox family.


FUNCTION: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADIPOR family.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4 subfamily.


SIMILARITY: To E.coli YdfK.


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


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. 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. 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: Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm, cytoskeleton, cilium basal body Note=Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules (By similarity). The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization (By similarity). SIMILARITY: Belongs to the ARL2BP family.


FUNCTION: Catalyzes the NAD-dependent oxidation of L-arabinitol to L- xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. NADP cannot act as a cosubstrate. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Accessory subunit of neuronal kainate-sensitive glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor channel activity, slowing the decay kinetics of the receptors, without affecting their expression at the cell surface, and increasing the open probability of the receptor channels. Modulates the agonist sensitivity of kainate receptors. Slows the decay of kainate receptor-mediated excitatory postsynaptic currents (EPSCs), thus directly influencing synaptic transmission (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single- pass type I membrane protein. SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Multi-pass membrane protein.


FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer. SIMILARITY: Belongs to the Rieske iron-sulfur protein family.


FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands (PubMed:31100221). Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis. Plays a key role in bile acid metabolism (By similarity). In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the sulfotransferase 1 family.


FUNCTION: Aldo-keto reductase; part of the gene cluster that mediates the biosynthesis of destruxins, insecticidal cyclic hexadepsipeptides which induce flaccid paralysis and visceral muscle contraction in insects through targeting the calcium channels and vacuolar-type ATPases (PubMed:22232661). The aldo-keto reductase dtxS3 converts alpha-ketoisocaproic acid from deaminated leucine into alpha- hydroxyisocaproic acid (HIC), which is the first substrate for destruxin assembly by dtxS1 (PubMed:22232661). L-aspartate decarboxylase dtxS4 converts aspartic acid into beta-alanine, the last substrate for the destruxin assembly line performed by dtxS1 (PubMed:22232661). The nonribosomal peptide synthetase dtxS1 synthesizes destruxins B and B2, whereas the cytochrome P450 monooxygenase dtxS2 is required to convert destruxin B into other destruxin derivatives, including destructins C, D, A and E (PubMed:22232661). Destruxin E-diol (ED) is further produced in a non- enzymatic manner from destruxin E (PubMed:22232661). Destruxins play an important role in virulence and escape from insect host immune defenses (PubMed:22232661). SIMILARITY: Belongs to the aldo/keto reductase family.


FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ITIH family.


FUNCTION: Involved in early stages of the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SWS1 family.


FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in glucose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


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


FUNCTION: Important for the activity of the AtzE subunit of 1- carboxybiuret hydrolase.


FUNCTION: Putative transcription factor. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Has a role in sporulation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Associates with the microtubule cytoskeleton.


FUNCTION: Required during early processes in pollen development. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and about 55 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. The capsid encapsulates the genomic DNA, but does not bind DNA. Essential for the initial attachment to the host cell (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the papillomaviridae L1 protein family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM41 family.


FUNCTION: Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Gustatory receptor (GR) family. Gr2a subfamily.


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. mL67/mhr1 also has extraribosomal functions, being involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells. mL67/mhr1 also acts as transcription factor involved in regulation of RNA polymerase II- dependent transcription. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL67 family.


FUNCTION: Involved in oocyte maturation. It is possible that D7 is required at a certain point in the maturation process and that maturation cannot proceed beyond this point unless a threshold amount of D7 protein is provided. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0224 (FAM112) family.


SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ElaB/YgaM/YqjD family.


SIMILARITY: Belongs to the HSBP1 family.


FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. SUBCELLULAR LOCATION: Plastid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. PsbC subfamily.


FUNCTION: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates. May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway. May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins. Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols. May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine- 1-phosphate. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Nucleus envelope Nucleus inner membrane. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family.


FUNCTION: Tyrosine protein phosphatase which functions as a dosage- dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro (By similarity). Phosphorylation by PIM1 leads to an increase in phosphatase activity (By similarity). SIMILARITY: Belongs to the MPI phosphatase family.


FUNCTION: Participates in both the initiation and recycling phases of transcription. In the presence of the delta subunit, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an increased efficiency of RNA synthesis because of enhanced recycling. SIMILARITY: Belongs to the RpoE family.


FUNCTION: Global regulator that is part of the nutrient-sensing system. In the absence of glucosamine 6-P (GlcN6P), represses the phosphotransferase system (PTS) specific for the uptake of N- acetylglucosamine (PTSNag), and genes involved in the metabolism of chitin, as well as several genes involved in development, thereby linking carbon availability to morphogenesis. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Effector that participates in the arbuscule development step of the symbiosis. Arbuscular mycorrhizal (AM) symbiosis is one of the most prominent and beneficial plant-microbe interactions that facilitates mineral nutrition and confers tolerance to biotic and abiotic stresses (PubMed:30233541). Is not involved in cell death processes (PubMed:30233541). SUBCELLULAR LOCATION: Secreted Host nucleus Note=Localizes to host nuclear bodies. SIMILARITY: Belongs to the Crinkler effector family.


FUNCTION: May be involved in the transport of sterols. SIMILARITY: Belongs to the OSBP family.


FUNCTION: Phosphatidylserine (PS) lipase that mediates the hydrolysis of phosphatidylserine to generate lysophosphatidylserine (LPS). LPS constitutes a class of signaling lipids that regulates immunological and neurological processes (By similarity). Has no activity towards diacylglycerol, triacylglycerol or lysophosphatidylserine lipase (By similarity). Also has monoacylglycerol lipase activity, with preference for 1-(9Z,12Z-octadecadienoyl)-glycerol (1-LG) and 2-glyceryl-15-deoxy- Delta(12,14)-prostaglandin J2 (15d-PGJ(2)-G) (By similarity). SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16 family.


FUNCTION: Immunity protein component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. Neutralizes the tRNase activity of cognate toxin WapA upon expression in E.coli. Does not inhibit WapA from other strains of B.subtilis. The WapA C-terminus cannot be expressed on its own in E.coli, however it can be cloned in the presence of its cognate immunity protein gene. Cell contact is probably necessary for growth inhibition.


FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:28502770, PubMed:29301961). Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-helicase activities of EIF4A3. Plays a role in the stress response by participating in cytoplasmic stress granules assembly and by favoring cell recovery following stress. Component of the dendritic ribonucleoprotein particles (RNPs) in hippocampal neurons. May play a role in mRNA transport. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Binds poly(G) and poly(U) RNA homomer. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Nucleus Nucleus speckle Cytoplasm, Stress granule Cytoplasm, Cytoplasmic ribonucleoprotein granule Cell projection, dendrite Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Transported to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA (PubMed:15166247). In nuclear speckles, colocalizes with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress granules (PubMed:17652158). In the dendrites of hippocampal neurons, localizes to dendritic ribonucleoprotein granules (By similarity). SIMILARITY: Belongs to the CASC3 family.


FUNCTION: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma family.


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.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0588 family.


FUNCTION: Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3- kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll- like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein.


FUNCTION: Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer). SIMILARITY: In the C-terminal section; belongs to the MurCDEF family.


FUNCTION: Transcriptional activator that binds specifically to the DNA sequence 5'-[AG]CCGAC-3'. Binding to the C-repeat/DRE element mediates cold-inducible transcription. CBF/DREB1 factors play a key role in freezing tolerance and cold acclimation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP2/ERF transcription factor family. ERF subfamily.


FUNCTION: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the pescadillo family.


FUNCTION: Krueppel is a gap class segmentation protein. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family.


FUNCTION: Required for disulfide bond formation in some proteins. Part of a redox system composed of DsbI and DsbL that mediates formation of an essential disulfide bond in AssT (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. DsbI subfamily.


FUNCTION: Protostadienol synthase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). Protostadienol synthase helA cyclizes (3S)- oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:19951700, PubMed:29158519). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). Following the cyclization to the tetracyclic protostadienol by helA, cytochrome P450 monooxygenases helB1-mediated and helB2-mediated oxidation at C-4 and C-16, acyltransferase helD2-dependent acetylation of 16-OH, oxidation of C-21 by cytochrome P450 monooxygenase helB4, and short chain dehydrogenase helC-dependent oxidative decarboxylation yield the fusidane skeleton (PubMed:29158519). This intermediate is further modified in three additional steps mediated by the cytochrome P450 monooxygenase helB3, the acyltransferase helD1, and the 3-ketosteroid 1-dehydrogenase helE to give helvolic acid (PubMed:19415934, PubMed:19216560, PubMed:29158519). Compared with the late stages in the biosynthesis of helvolic acid, enzymes involved in the early stage modifications act in a relatively strict order (PubMed:29158519). The hydroxylation of C-16 by helB1 and subsequent acetylation by helD2 should occur before the helB3-mediated oxidation of C-21 (PubMed:29158519). C-4 demethylation in fusidane-type antibiotics proceeds in an unusual manner though it is also achieved by oxidative decarboxylation (PubMed:19415934, PubMed:29158519). The methyl group at C-4 beta position is oxidized by helB1 and subsequently removed by the short chain dehydrogenase helC (PubMed:19415934, PubMed:29158519). FUNCTION: Protostadienol synthase which cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol), the biosynthetic precursor of helvolic acid, a secondary metabolite which promotes virulence. SIMILARITY: Belongs to the terpene cyclase/mutase family.


FUNCTION: Acts with sax-2 to restrict the growth of both primary and secondary neurites. Regulates mechanosensory tiling by controlling the termination point of sensory dendrites. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.


FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR) signaling. SIMILARITY: Belongs to the lst-2 family.


SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the Lactobacillus delbrueckii bacteriophages Gp34 family.


FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1- RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2 (By similarity). FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1- RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) direct ubiquitination of BCL2. SIMILARITY: Belongs to the SKP1 family.


FUNCTION: Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2. Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Apical cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues. Plays a role in oxidative stress resistance (PubMed:23438705). Might promote neuronal cell death under ischemic conditions and cell death in touch neurons induced by mec-4 channel hyperactivation, possibly downstream of the insulin-like receptor daf-2 (PubMed:28820880). Might attenuate the reactive oxygen species (ROS) scavenging system, that eliminates ROS in ischemic conditions, under dietary deprivation and when glycolysis is blocked (PubMed:28820880). SUBCELLULAR LOCATION: Mitochondrion matrix Mitochondrion. SIMILARITY: Belongs to the sirtuin family. Class II subfamily.


SIMILARITY: Belongs to the polysaccharide pyruvyl transferase family.


SIMILARITY: Belongs to the SPATA2 family.


FUNCTION: Has alanine:glyoxylate aminotransferase activity. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking (By similarity). Essential for the formation of the sequestering membranes and assembly of the micropexophagy-specific membrane apparatus (MIPA) which mediates the fusion of the sequestering membranes and incorporation of the peroxisomes into the vacuole during micropexophagy (PubMed:11533052, PubMed:16079180). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=The peripheral pool of ATG9 partially colocalizes with mitochondria and it has been speculated that ATG9 resides either in the mitochondria or within vesicles in very close to the mitochondria. During methanol growth, localizes to multiple structures situated near the plasma membrane referred as the peripheral compartment (Atg9-PC). During glucose-induced micropexophagy, traffics from the Atg9-PC to unique perivacuolar structures (PVS) that contain ATG11, but lack ATG2 and ATG8. SIMILARITY: Belongs to the ATG9 family.


FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate in the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators (By similarity) (PubMed:22216341, PubMed:23873268). In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell projection, dendrite Note=In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree. SIMILARITY: Belongs to the ELO family. ELOVL5 subfamily.


FUNCTION: In molluscan muscle, calcium regulation is associated with myosin rather than with actin. Muscle myosin contains two types of light chains: the catalytic light chain, essential for ATPase activity, and the regulatory light chain, a calcium-binding protein responsible for Ca(2+) dependent binding and Ca(2+) dependent Mg-ATPase activity.


FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:17112342). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:17112342). Catalyzes predominantly the oxidation of the terminal carbon (omega- oxidation) of saturated and unsaturated fatty acids (PubMed:17112342). May act as a major omega-hydroxylase for dodecanoic (lauric) acid in kidney (PubMed:17112342). Participates in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20- hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Further catalyzes successive omega-oxidations of 20-HETE to the corresponding dicarboxylic acid, and may contribute to the degradation of PUFA by chain shortening (PubMed:17112342). Acts as an omega-hydroxylase and epoxidase toward (5Z,8Z,11Z,14Z,17Z)- eicosapentaenoc acid (EPA). Catalyzes stereoselective epoxidation of the last double bond of EPA, displaying a strong preference for the (R,S) stereoisomer (PubMed:17112342). Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency (PubMed:17112342). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively. FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the N-terminal section; belongs to the pantothenate synthetase family. SIMILARITY: In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AAA ATPase family.


FUNCTION: Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. Participates in the interaction between the capsid and the tegument through interaction with the large tegument protein/LTP. SUBCELLULAR LOCATION: Virion Host nucleus. SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae CVC2 protein family.


FUNCTION: RNA-binding factor which binds specifically to the very 3'- UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=PIPPin-RNA complexes are located to the nucleus.


FUNCTION: RNA-binding protein which may be involved in spermatogenesis. Required for sperm development, possibly by participating in pre-mRNA splicing in the testis. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Involved in the differentiation of haploid spermatids.


SIMILARITY: Belongs to the IIV-6 170L family.