FUNCTION: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Required to direct preproteins in transit and direct them to the channel protein TIM23, and possibly facilitates transfer of the translocating proteins from the TOM complex to the TIM23 complex (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TIM50 family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL34 family.


FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily.


FUNCTION: The VP7 protein is one of the five proteins (with VP1, VP3, VP4, and VP6) which form the inner capsid of the virus. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the orbivirus VP7 family.


FUNCTION: Malate synthase which takes part in the glyoxylate cycle (PubMed:1454530). MLS1 activity is essential for cells to grow on oleic acid as a sole carbon source (PubMed:11846793). Two steps of the glyoxylate cycle take place in the cytosol, the splitting of isocitrate into succinate and glyoxylate, and the dehydrogenation of malate to oxaloacetate (PubMed:1454530). However, the formation of malate from glyoxylate and acetyl-CoA undertaken MLS1, occurs in the peroxisomes when cells are grown on oleic acid (Probable). The source of acetyl-CoA being either peroxisomal when breaking down fatty acids, or cytosolic when extra-cellular two-carbon substrates are used, therefore, although not strictly essential, the peroxisomal localization of MLS1 appears to be advantageous for cells growing on oleic acid, in that acetyl-CoA production and utilization are thereby intimately compartmentalized together to increase efficiency (Probable). SUBCELLULAR LOCATION: Peroxisome matrix Note=Imported in peroxisome via recognition by the peroxisomal targeting signal receptor PEX9 in an oleate-dependent manner. SIMILARITY: Belongs to the malate synthase family.


SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.


FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PlsY family.


FUNCTION: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Sulfate/tungstate importer (TC 3.A.1.6) family.


FUNCTION: Specifically methylates the N7 position of guanine in position 518 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.


FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Secreted, capsule Cell surface Secreted, cell wall. SIMILARITY: Belongs to the chaperonin (HSP60) family.


FUNCTION: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of DRE2, another key component of the CIA machinery. In turn, this reduced cluster provides electrons for assembly of cytosolic iron-sulfur cluster proteins. Positively controls H(2)O(2)-induced cell death. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion Note=Relocalizes to mitochondria after H(2)O(2) exposure. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. SIMILARITY: Belongs to the NADPH-dependent diflavin oxidoreductase NDOR1 family. SIMILARITY: In the N-terminal section; belongs to the flavodoxin family.


FUNCTION: Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L- tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety. SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.


FUNCTION: Required for rescue of stalled ribosomes mediated by trans- translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans- translation. SUBCELLULAR LOCATION: Cytoplasm Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. SIMILARITY: Belongs to the SmpB family.


FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Cytoplasm Secreted Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion.


FUNCTION: Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback- inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family.


FUNCTION: Adenosylhomocysteine is a competitive inhibitor of S- adenosyl-L-methionine-dependent methyl transferase reactions; therefore adenosylhomocysteinase may play a key role in the control of methylations via regulation of the intracellular concentration of adenosylhomocysteine. SIMILARITY: Belongs to the adenosylhomocysteinase family.


SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family.


FUNCTION: May play a role in regulating cell adhesion/migration complexes in migrating cells. SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus Cell projection, lamellipodium Note=Colocalized with EZR/VIL2, actin and CD44 in lamellipodia. SIMILARITY: Belongs to the protein kinase superfamily.


FUNCTION: Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C- terminal domain of GyrB, which probably disrupts DNA binding by the gyrase. SIMILARITY: Belongs to the DNA gyrase inhibitor YacG family.


SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase A1 family.


FUNCTION: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fluoride channel Fluc/FEX (TC 1.A.43) family.


FUNCTION: Promotes megakaryocyte differentiation by enhancing ERK phosphorylation and up-regulating RUNX1 expression. SUBCELLULAR LOCATION: Cytoplasm Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family.


SUBCELLULAR LOCATION: Secreted, cell wall.


FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MetA family.


FUNCTION: Kissper is an anion-selective pore-forming peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kiwellin family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family.


FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the chaperonin (HSP60) family.


FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family.


FUNCTION: One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome. SIMILARITY: Belongs to the universal ribosomal protein uL23 family.


SIMILARITY: Belongs to the UPF0260 family.


FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the TolB family.


SIMILARITY: Belongs to the WrbA family.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase subfamily.


FUNCTION: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RuvB family.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3- methylorsellinate into nidulol (PubMed:24244835). CicB converts 3- methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine (PubMed:24244835). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: RNA-dependent RNA polymerase which replicates the viral genome.


FUNCTION: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the elongation factor P family.


FUNCTION: Has antibacterial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family.


SIMILARITY: Belongs to the elongation factor P family.


FUNCTION: Protein that assembles into highly ordered structures and provides a specific site for viral DNA replication. Probably anchors the viral DNA replisome to the host membrane. SUBCELLULAR LOCATION: Host membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phi29likevirus DNA replication protein 1 family.


FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3- phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.


FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.


FUNCTION: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methylthiotransferase family. MiaB subfamily.


FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific endoribonuclease. Involved in the integration of spacer DNA into the CRISPR cassette. SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2 protein family.


FUNCTION: Probable toxin that inhibits ion channels. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily.


FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. FUNCTION: Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class I family.


FUNCTION: Involved in bleomycin tolerance with links to DNA repair and/or proteasome function. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CUB1 family.


FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family. SIMILARITY: In the N-terminal section; belongs to the flavodoxin family. SIMILARITY: Belongs to the NADPH-dependent sulphite reductase flavoprotein subunit CysJ family.


FUNCTION: Mediates the binding and degradation of acetylated low density lipoprotein (Ac-LDL). Mediates heterophilic interactions, suggesting a function as adhesion protein. Plays a role in the regulation of neurite-like outgrowth (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic acid exporter ArAE (TC 2.A.85) family.


FUNCTION: Core component of the TRAPP complexes which has a function of guanine nucleotide exchange factor activity for Rab1 GTPase. Plays a role in vesicular transport from endoplasmic reticulum to Golgi and autophagy (By similarity). May play a role in dendrite postsynaptic membrane trafficking (By similarity). FUNCTION: Core component of the TRAPP complexes which has a function of guanine nucleotide exchange factor activity for Rab1 GTPase (Probable). Plays a role in vesicular transport from endoplasmic reticulum to Golgi and autophagy (PubMed:31794024). May play a role in dendrite postsynaptic membrane trafficking (By similarity). SUBCELLULAR LOCATION: Postsynaptic cell membrane Golgi apparatus membrane Endoplasmic reticulum Vesicle Note=Associated with postsynaptic membranes and in intracellular cisterns and vesicles (Golgi). SIMILARITY: Belongs to the TRAPP small subunits family. TRAPPC4 subfamily.


FUNCTION: [Capsid protein alpha]: Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, 240 calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid protein alpha generating capsid protein beta and the membrane-active peptide gamma. FUNCTION: [Membrane-lytic peptide gamma]: Membrane-permeabilizing peptide produced by virus maturation, thereby creating the infectious virion. After endocytosis into the host cell, peptide gamma is probably exposed in endosomes, where it permeabilizes the endosomal membrane, facilitating translocation of viral capsid or RNA into the cytoplasm. Involved in specific recognition and packaging of viral RNA during assembly. SUBCELLULAR LOCATION: [Membrane-lytic peptide gamma]: Virion Note=located inside the capsid. SUBCELLULAR LOCATION: [Capsid protein beta]: Virion. SIMILARITY: Belongs to the peptidase A6 family.


FUNCTION: Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown (By similarity). SUBCELLULAR LOCATION: Cell projection, cilium membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Mainly localizes to primary cilium in a TULP3 and IFT-A complex-dependent manner. In presence of SHH, it is removed from primary cilia and is internalized into recycling endosomes and is apparently not degraded (By similarity). SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage between the phosphate and headgroup of certain phospholipids (sphingolipid and lysolipid substrates), forming an alcohol (often choline) and a cyclic phosphate (By similarity). This toxin acts on sphingomyelin (SM) (By similarity). It may also act on ceramide phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by transphosphatidylation, releasing exclusively cyclic phosphate products as second products (By similarity). Induces dermonecrosis, hemolysis, increased vascular permeability, edema, inflammatory response, and platelet aggregation (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the arthropod phospholipase D family. Class II subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsA family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase subfamily.


SUBCELLULAR LOCATION: Secreted.


FUNCTION: Glutathione S-transferase that catalyzes the conjugation of glutathione to exogenous and endogenous compounds (PubMed:14709161, PubMed:14742434). Significant glutathione conjugating activity is found only with the model substrate, 1-chloro-2,4-dinitrobenzene (CDNB) (PubMed:14709161). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the GST superfamily. Kappa family.


FUNCTION: Located on the platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS11 family.


FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LipB family.


FUNCTION: May act as an inhibitor of TGF-beta signaling. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily.


SIMILARITY: Belongs to the OMP decarboxylase family. Type 2 subfamily.


SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.


SIMILARITY: Belongs to the mimivirus L17x/L18x family.


FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family.


FUNCTION: Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PIGL family.


FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily.


FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin. In vitro catalyzes the oxidation of both enantiomers of naringenin to give both cis- and trans-dihydrokaempferol. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.


FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. SIMILARITY: Belongs to the cyanase family.


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


FUNCTION: Putative transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase family.


FUNCTION: Phosphorelay intermediate protein that is part of the branched SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound osmosensing histidine kinase SLN1 to two distinct response regulator proteins, SSK1 in the cytoplasm, and transcription factor SKN7 in the nucleus. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes constitutively to the cytoplasm and the nucleus, independent on osmotic conditions and phosphorylation status of the protein. SIMILARITY: Belongs to the YPD1 family.


FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. Also serves as the primary chemoreceptor for chemotaxis. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.


FUNCTION: Involved in the trafficking of vacuolar proteins. May function as a sorting receptor for protein trafficking to the protein storage vacuole (PSV) (By similarity). SUBCELLULAR LOCATION: Prevacuolar compartment membrane Protein storage vacuole membrane; Single-pass type I membrane protein.


FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5- phosphate. SIMILARITY: Belongs to the FGGY kinase family.


FUNCTION: B6-vitamer kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5'-phosphorylated esters, i.e. PNP, PLP and PMP. SIMILARITY: Belongs to the pyridoxine kinase family. PdxK subfamily.


SUBCELLULAR LOCATION: Nucleus.


FUNCTION: May be involved in the proteolytic processing of a quorum sensing system signal molecule precursor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AgrB family.


FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of three isoenzymes responsible for cellular hyaluronan synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Cytoplasmic vesicle Note=Travels through endoplasmic reticulum (ER), Golgi, plasma membrane, and endocytic vesicles (PubMed:16014622). Actives only when present in plasma membrane (PubMed:16014622). O-GlcNAcylation controls its membrane localization (By similarity). A rapid recycling of HAS3 between plasma membrane and endosomes is controlled by the cytosolic levels of UDP-GlcUA and UDP- GlcNAc (By similarity). SIMILARITY: Belongs to the NodC/HAS family.


SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.


FUNCTION: Catalyzes the incorporation of the first glycine of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. This glycine is added to the epsilon-amino group of the L-lysine of the membrane-bound lipid II intermediate (GlcNAc-(beta-1,4)-N-acetylmuramic acid(-L-Ala-D-iGln-L-Lys-D-Ala-D- Ala)-pyrophosphoryl-undecaprenol), using glycyl-tRNA(Gly) as donor, in a ribosome-independent mechanism. Involved in methicillin resistance (By similarity). FUNCTION: Catalyzes the incorporation of the first glycine of the pentaglycine interpeptide bridge, which is characteristic of the S.aureus peptidoglycan. This glycine is added to the epsilon-amino group of the L-lysine of the membrane-bound lipid II intermediate (GlcNAc-(beta-1,4)-N-acetylmuramic acid(-L-Ala-D-iGln-L-Lys-D-Ala-D- Ala)-pyrophosphoryl-undecaprenol), using glycyl-tRNA(Gly) as donor, in a ribosome-independent mechanism. Involved in methicillin resistance. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FemABX family.


FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)- succinylornithine, ammonia and CO(2). SIMILARITY: Belongs to the succinylarginine dihydrolase family.


FUNCTION: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FBPase class 1 family.


FUNCTION: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. Retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) (By similarity). Acts also as component of the retriever complex. The retriever complex is an heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrins. In the endosomes, retriever complex drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the VPS29 family.


FUNCTION: A putative specificity subunit for a type I restriction enzyme; the corresponding endonuclease and methylase subunits have multiple frameshifts and are probably not expressed. SIMILARITY: Belongs to the type-I restriction system S methylase family.


SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family.


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


FUNCTION: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the expansin family. Expansin A subfamily.


FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA). SIMILARITY: Belongs to the LpxK family.


FUNCTION: Probably part of an ABC transporter complex. Responsible for energy coupling to the transport system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARF family.


FUNCTION: Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI). SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.


FUNCTION: Activates expression of the rhaSR operon in response to L- rhamnose. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the IlvD/Edd family.


FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family.


FUNCTION: One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IF-1 family.


FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.


FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. May have an important role in maintaining immune self-tolerance (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the SAPS family.


FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.


FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cL37 family.


FUNCTION: Probably participates in a plant defense mechanism. SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1 subfamily.


FUNCTION: Required for maturation of 30S ribosomal subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RimP family.


FUNCTION: Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Increases the RNA binding and the efficiency of RNA degradation. Confers strong poly(A) specificity to the exosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RRP4 family.


FUNCTION: Involved in the export and assembly of pili subunits across the outer membrane. Forms a hexameric ring-shaped pore in the outer bacterial membrane. The 2 nanometer-diameter pore allows the passage of the thin tip fibrillum. As for the rod, it probably unwinds into linear fibers which would therefore be narrow enough to pass through the pore. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. FUNCTION: With S5 and S12 plays an important role in translational accuracy. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS4 family.


FUNCTION: TP and TP5 may play a role in T-cell development and function. TP5 is an immunomodulating pentapeptide. FUNCTION: May be involved in the structural organization of the nucleus and in the post-mitotic nuclear assembly. Plays an important role, together with LMNA, in the nuclear anchorage of RB1. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Expressed diffusely throughout the nucleus. SIMILARITY: Belongs to the LEM family.


FUNCTION: Involved in glutaminase-dependent acid resistance. Exchanges extracellular glutamate (Glu) for intracellular gamma-aminobutyric acid (GABA) under acidic conditions. The ability to survive the extremely acidic conditions of the stomach is essential for successful colonization of the host by commensal and pathogenic bacteria. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Glutamate:GABA antiporter (GGA) (TC 2.A.3.7) family.


FUNCTION: Catalyzes DNA synthesis. SIMILARITY: Belongs to the DNA polymerase type-B family.


FUNCTION: Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FliW family.


FUNCTION: Plays a major role in protein secretion by helping the post- translocational extracellular folding of several secreted proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the PrsA family.


FUNCTION: Component of a transcriptional repressor complex together with MAX (By similarity). In complex with MAX binds to the core DNA sequence 5'-CAC[GA]TG-3' (By similarity). Antagonizes MYC transcriptional activity by competing with MYC for MAX binding (By similarity). Binds to the TERT promoter and represses telomerase expression, possibly by interfering with MYC binding (By similarity). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Involved in the biosynthesis of the antifungal agent validamycin A (PubMed:16725283). Catalyzes the dephosphorylation of validoxylamine A 7'-phosphate to yield validoxylamine A (PubMed:21766819). VldH is also able to convert trehalose 6-phosphate to trehalose (PubMed:21766819). SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.


SIMILARITY: Belongs to the universal ribosomal protein uS2 family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM19 family.


FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.


FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. FUNCTION: Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release. SIMILARITY: Belongs to the universal ribosomal protein uL1 family.


FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins. SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein Host Golgi apparatus membrane; Multi-pass membrane protein Note=Largely embedded in the lipid bilayer. SIMILARITY: Belongs to the alphacoronaviruses M protein family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.


FUNCTION: The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapid growth inhibition, cell wall depositions and accumulation of defense-related transcripts. This protein is required for responses to chitin and acts redundantly with MEKK1a. SUBCELLULAR LOCATION: Cell membrane. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.


FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.


FUNCTION: Part of the accessory SecA2/SecY2 system specifically required to export GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon. SIMILARITY: Belongs to the accessory Sec system protein Asp2 family.


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


FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfamily.


FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- dihydropteroate (H2Pte), the immediate precursor of folate derivatives. SIMILARITY: Belongs to the DHPS family.


FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.


FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex (By similarity). SIMILARITY: Belongs to the CENP-L/IML3 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family.


FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 28 family.


FUNCTION: This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. SIMILARITY: Belongs to the universal ribosomal protein uL13 family.


FUNCTION: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the COX15/CtaA family. Type 2 subfamily.


FUNCTION: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. HisZ subfamily.


FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KdsB family.


FUNCTION: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CoaE family.


FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A. SIMILARITY: Belongs to the CbiD family.


SIMILARITY: Belongs to the bacterial ribosomal protein bL17 family.


SIMILARITY: Belongs to the peptidase S15 family.


FUNCTION: ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ClpX chaperone family. HslU subfamily.


FUNCTION: May have an RNA/DNA binding role.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS8 family.


FUNCTION: Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Cell junction Cytoplasmic vesicle membrane Note=Localizes to RAB13-positive vesicles and to the plasma membrane at intercellular contacts.


FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids. SIMILARITY: Belongs to the UPP synthase family.


FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD kinase family.


FUNCTION: Probably acts as an electrical shunt for an outwardly- directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClcB subfamily.


FUNCTION: This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. SIMILARITY: Belongs to the universal ribosomal protein uL18 family.


FUNCTION: Catalyzes the isomerization of 5-dehydro-4-deoxy-D- glucuronate to 3-deoxy-D-glycero-2,5-hexodiulosonate. SIMILARITY: Belongs to the KduI family.


FUNCTION: Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-4/IL-13 family.


FUNCTION: May play a role in neurite outgrowth and neurogenesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, neuron projection. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family.


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


FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.


SIMILARITY: Belongs to the UPF0297 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 turnover 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(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase epsilon chain family.


FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.


FUNCTION: [Isoform 2]: Functions as transcription repressor; isoform 2 has lower transcription repressor activity than isoform 1 and isoform 3. FUNCTION: [Isoform 1]: Functions as transcription repressor, probably via its interaction with histone deacetylase complexes (PubMed:16820529, PubMed:18070604). Involved in the functional recruitment of the class 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus (PubMed:16820529). Binds DNA, apparently without sequence-specificity, and bends bound double-stranded DNA (PubMed:19015240). Binds phosphoinositol phosphates (phosphoinositol 3- phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate) via the same basic sequence motif that mediates DNA binding and nuclear import (PubMed:19015240, PubMed:26609676). FUNCTION: [Isoform 3]: Functions as transcription repressor; its activity is marginally lower than that of isoform 1. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus. SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleolus. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleolus. SIMILARITY: Belongs to the SAP30 family.


FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor. May play a role in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Lysosome membrane Note=Localizes to the centrosomes in a microtubule-dependent manner. SIMILARITY: Belongs to the BLOC1S2 family.


FUNCTION: Together with PDP1, PDP2 and PDP6, interacts with MSI4/FVE and MSI5 to suppress FLC, MAF4 and MAF5 expression by regulating the function of the PRC2 complex and modulating H3K27me3 level, thereby promoting flowering. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PDP family.


FUNCTION: One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. IF-2 subfamily.


FUNCTION: Binds as a heterodimer with protein bS6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.


FUNCTION: Could be a 3Fe-4S cluster-containing protein. Probably participates in a redox process with YgcN, YgcQ and YgcR. SIMILARITY: Belongs to the bacterial-type ferredoxin family. FixX subfamily.


FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family.


FUNCTION: Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5- trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, PML body Cell projection, dendritic spine Postsynaptic density. SIMILARITY: Belongs to the PTEN phosphatase protein family.


FUNCTION: Part of a group II capsule biosynthesis locus. SIMILARITY: Belongs to the stealth family.


FUNCTION: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity (By similarity). In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin (By similarity). In the central nervous system, it is involved in the regulation of neurite formation and arborization (PubMed:30184290). It may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning (PubMed:30184290). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK- STAT signaling pathway (PubMed:11972023). SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.


FUNCTION: Alpha-L-arabinofuranosidase 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. Releases L-arabinose from arabinoxylan (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 62 family.


FUNCTION: Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Note=Covalently-linked to the cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 17 family.


FUNCTION: Strong activator of the late viral genes promoters. Acts as a suppressor of RNA-mediated gene silencing, also known as post- transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. TrAP suppresses the host RNA silencing by inhibiting adenosine kinase 2 (ADK2), a kinase involved in a general methylation pathway. Also suppresses the host basal defense by interacting with and inhibiting SNF1 kinase, a key regulator of cell metabolism implicated in innate antiviral defense. Determines pathogenicity (By similarity). SUBCELLULAR LOCATION: Host nucleus Host cytoplasm Note=The phosphorylated form appears to accumulate almost exclusively in the nucleus, whereas the non-phosphorylated form is found in both nucleus and cytoplasm. SIMILARITY: Belongs to the geminiviridae transcriptional activator protein family.


FUNCTION: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Methionine importer (TC 3.A.1.24) family.


FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Rab9 effector required for endosome to trans-Golgi network (TGN) transport.


FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). SIMILARITY: Belongs to the IPP transferase family.


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


FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ThiG family.


FUNCTION: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the R-transferase family. Bpt subfamily.


FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F- actin) and binds to actin monomers (PubMed:15563618, PubMed:19794115). Required for normal cell growth, plant development, cell organ expansion and flowering. Essential for root-knot nematode infection (PubMed:19794115). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin-binding proteins ADF family.


FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H4 family.


FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL14 family.


FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. SIMILARITY: Belongs to the universal ribosomal protein uL24 family.


FUNCTION: Maintains high levels of reduced glutathione in the cytosol. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family.


FUNCTION: Catalyzes the activation of long-chain fatty acids as acyl- adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase PpsA for further chain extension (PubMed:15042094, PubMed:15749014, PubMed:20553505). Catalyzes the adenylation of the long-chain fatty acids eicosanoate (C20) or docosanoate (C22), and potentially the very-long-chain fatty acid lignocerate (C24) (PubMed:15749014, PubMed:20553505). Involved in the biosynthesis of phthiocerol dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B) (PubMed:11279114, PubMed:20553505). FUNCTION: Catalyzes the activation of long-chain fatty acids as acyl- adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase PpsA for further chain extension. Catalyzes the adenylation of the long-chain fatty acids eicosanoate (C20) or docosanoate (C22), and potentially the very-long-chain fatty acid lignocerate (C24). Involved in the biosynthesis of phthiocerol dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA. SIMILARITY: Belongs to the universal ribosomal protein uS7 family.


FUNCTION: Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the virgaviridae capsid protein family.


FUNCTION: Effector component of the propane 2-monooxygenase multicomponent enzyme system which is involved in the degradation of propane via the O2-dependent hydroxylation of propane. SIMILARITY: Belongs to the TmoD/XamoD family.


FUNCTION: Part of a sulfur-relay system required for 2-thiolation of 5- methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DsrF/TusC family.


FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. SIMILARITY: Belongs to the TrpA family.


FUNCTION: Exhibits stronger antimicrobial activity against the Gram- positive bacteria (S.aureus (IC(50) is 7.4 ug/ml)) and fungi (C.albicans (IC(50) is 3.0 ug/ml) and P.pastoris (IC(50) is 0.1 ug/ml)) than Gram-negative bacteria (E.coli no inhibition at 100 ug/ml). Binds to chitin (4.3 uM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre- mRNA splicing. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC15 family.


FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.


FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely associated with the inner membrane. SIMILARITY: Belongs to the cytochrome c family.


FUNCTION: Probably involved in the transfer of reducing equivalents from stroma to thylakoid lumen and required for the biogenesis of the plastid cytochrome b6f complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbD family.


FUNCTION: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the peptidase S26B family.


FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl- PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with the membrane possibly through PlsY. SIMILARITY: Belongs to the PlsX family.


FUNCTION: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network. SUBCELLULAR LOCATION: Host nucleus inner membrane; Single-pass membrane protein Note=Localizes also at the transient membrane of perinuclear virions. SIMILARITY: Belongs to the herpesviridae NEC2 protein family.


FUNCTION: Transcriptional regulator; part of the gene cluster that mediates the biosynthesis of pyriculol and pyriculariol, two heptaketides that induce lesion formation upon application on rice leaves but are dispensable for pathogenicity (PubMed:27902426). With TRF2, negatively regulates the expression of the gene cluster and the subsequent pyriculol and pyriculariol production (PubMed:27902426). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. SIMILARITY: Belongs to the universal ribosomal protein uL6 family.


FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. SIMILARITY: Belongs to the type A lantibiotic family.


FUNCTION: Serine/threonine haspin-like protein kinase involved in cell cycle regulation. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Haspin subfamily.


FUNCTION: Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.


FUNCTION: Chaperone of the type III secretion (T3S) injectisome that translocates effector toxins into host cells, facilitating the establishment and dissemination of infection. Prevents premature polymerization of PscF, along with PscG, within the cytoplasm (PubMed:20494986). Required for type III secretion needle assembly. Also required for cytotoxicity by influencing PscF levels. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YscE family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0761 family.


FUNCTION: Regulatory subunit of S-adenosylmethionine synthetase 2, an enzyme that catalyzes the formation of S-adenosylmethionine from methionine and ATP. Regulates MAT2A catalytic activity by changing its kinetic properties, increasing its affinity for L-methionine. Can bind NADP (in vitro). SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family. MAT2B subfamily.


FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate. SIMILARITY: Belongs to the LamB/PxpA family.


FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). Plays a role in spermatogenesis (PubMed:24557841). In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (PubMed:24557841). FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. In the ATP- bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Note=Colocalizes with SHCBP1L at spindle during the meiosis process. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Note=Colocalizes with SHCBP1L at spindle during the meiosis process (PubMed:24557841). SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Involved in the biosynthesis of mycolic acids (By similarity). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (By similarity). Can use decanoate (C10), dodecanoate (C12) and tetradecanoate (C14) (PubMed:23364516, PubMed:26900152). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. SIMILARITY: Belongs to the alanine racemase family.


FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of estradiol and estrone. May play a role in the regulation of estrogen receptor activity by metabolizing free estradiol (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfotransferase 1 family.


SIMILARITY: Belongs to the universal ribosomal protein uL30 family.


FUNCTION: This enzyme can effectively convert cephalosporin C into 7- beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the DAMOX/DASOX family.


FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SIMILARITY: Belongs to the SEC6 family.


FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease III family.


FUNCTION: Counteracts the host humoral immune response by inhibiting the processing and the amidolytic activity of host PAP1 and PAP3. Thereby, melanization of host hemolymph, normally producing several reactive intermediates toxic for viruses, is deregulated and proper immune response cannot occur (By similarity). SIMILARITY: Belongs to the polydnaviridae EGF-like motif protein family.


FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PNP/UDP phosphorylase family.


FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. SIMILARITY: Belongs to the globin family.


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


FUNCTION: Cytoskeletal linker that plays a central role in the flagellum cell motility. Required for directional cell motility. Plays a role as part of a dynein regulatory system that regulates flagellar beat in response to signals from the central pair apparatus and radial spokes in procyclic cells. Also plays an essential role in the bloodstream form of the trypanosomes as its silencing is lethal for the circulating form. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, cilium, flagellum. Note=Associated with the cytoskeleton. Localized to the site of attachment of the flagellum to the subpellicular cytoskeleton. Also localized in the flagellum of the bloodstream form trypanosomes. SIMILARITY: Belongs to the DRC4 family.


FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UppP family.


FUNCTION: May play a role in genome packaging through direct interaction with viral DNA. Binds to ssDNA and dsDNA with the same apparent affinity in vitro. SUBCELLULAR LOCATION: Virion Note=Found in association with the viral nucleoid. SIMILARITY: Belongs to the asfivirus P10 family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bS18 family.


FUNCTION: Downstream effector molecule involved in the transmission of signals from tyrosine kinase receptors and small GTPases to the actin cytoskeleton. Promotes formation of actin filaments. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex (By similarity). As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity). Also involved in the regulation of mitochondrial dynamics (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Synapse Cell junction, focal adhesion Note=Dot- like pattern in the cytoplasm. Concentrated in Rac-regulated membrane- ruffling areas. Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2. In neurons, colocalizes with activated NTRK2 after BDNF addition in endocytic sites through the association with TMEM108 (By similarity). SIMILARITY: Belongs to the SCAR/WAVE family.


FUNCTION: Acts as an extracellular morphogen to establish at least two cellular response thresholds within the dorsal half of the drosophila embryo. Required for the proper development of the embryonic dorsal hypoderm, for viability of larvae and for cell viability of the epithelial cells in the imaginal disks. Acts together with scw (By similarity). SUBCELLULAR LOCATION: Secreted. Note=Is internalized by receptor- mediated endocytosis. SIMILARITY: Belongs to the TGF-beta family.


FUNCTION: Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. SIMILARITY: Belongs to the activator 1 small subunits family. RfcL subfamily.


FUNCTION: Orphan receptor activated by a subset of RFamide-family neuropeptides such as FLRF-amide and FMRF-amide. Mediates its action by association with G proteins that activate a phosphatidylinositol- calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. May regulate the function of nociceptive neurons by modulation of pain perception. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily.


FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate importer (TC 3.A.1.7) family.


FUNCTION: Anticoagulant protein which binds to the gamma- carboxyglutamic acid-domain regions of factors IX (F9) and factor X (F10) in the presence of calcium with a 1 to 1 stoichiometry. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family.


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


FUNCTION: Involved in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Can use L-valine or L-isoleucine as substrate, but not L-leucine, L-phenylalanine, L-tyrosine, D-valine or D-isoleucine. SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the urease beta subunit family.


FUNCTION: Antibacterial peptide with wide spectrum of activity. Active against L.lactis, L.innocua, M.luteus, S.uberis and less against P.multocida and S.epidermidis. FUNCTION: Antibacterial peptide with wide spectrum of activity. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.


SIMILARITY: Belongs to the glycosyl hydrolase 32 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0397 family.


FUNCTION: Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component or to other electron acceptors such as cytochrome c and Fe(3+) ion. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family. HpaC subfamily.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 5 family.


FUNCTION: Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. SIMILARITY: Belongs to the protein prenyltransferase subunit beta family.


FUNCTION: Snake venom serine protease that may impair the hemostatic system of the prey. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.


FUNCTION: Transcriptional coactivator; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer neosartorin, which exhibits antibacterial activity. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln). SIMILARITY: Belongs to the GatC 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. Minor subunit located with subunit a in the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase protein 8 family.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). SIMILARITY: Belongs to the amidase family. GatA subfamily.


FUNCTION: Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors. SUBCELLULAR LOCATION: Nucleus. Chromosome.


FUNCTION: Binds voltage-dependently at site 3 of sodium channels (Nav) and inhibits the inactivation, thereby blocking neuronal transmission (By similarity). The minimum lethal dose against crabs is 7.3 mg/kg (Ref.1). SUBCELLULAR LOCATION: Secreted. Nematocyst. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type I subfamily.


FUNCTION: Has broad-spectrum antimicrobial properties. Has antibacterial activity against the Gram-positive bacterium L.monocytogenes EGD and the Gram-negative bacteria E.coli ML-35p and avirulent S.typhimurium 7953, but not against the mouse-virulent S.typhimurium 14028S. Probably contributes to the antimicrobial barrier function of the small bowel mucosa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family.


FUNCTION: Catalyzes the formation of 5-methyl-uridine at position 1939 (m5U1939) in 23S rRNA. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmD subfamily.


FUNCTION: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane (PubMed:11880379). The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=ocalized at the brush border membrane in the kidney. SIMILARITY: Belongs to the SLC34A transporter family.


FUNCTION: GATA-type transcription repressor that regulates iron- acquisition genes through specific binding the GATA sequence element 5'-(G/A)ATC(T/A)GATAA-3' of target promoters in an iron- and zinc-dependent manner (PubMed:18549241, PubMed:22117028). Regulation occurs via direct binding of iron ions (PubMed:18549241). Iron acquisition regulation is critical for survival under both iron- limiting conditions (to acquire essential iron) and iron-replete conditions (to limit iron toxicity) (PubMed:22117028). SRE1 targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis, presumed ferric reductase activity, iron-responsive transcriptional regulation, oxidative stress response, as well as genes encoding a number of putative oxidoreductases, metabolic and mitochondrial enzymes, superoxide dismutase, and genes previously identified as induced during nitrosative stress (PubMed:22117028). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Precursor of the major egg-yolk proteins that are sources of nutrients during early development of oviparous organisms.


FUNCTION: Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. SIMILARITY: Belongs to the Fmt family.


FUNCTION: Involved in DNA double-strand break (DSB) repair (PubMed:12052775). Acts probably with HerA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits both single-stranded endonuclease activity and 5'-3' exonuclease activity on single-stranded and double-stranded DNA (PubMed:12052775). SIMILARITY: Belongs to the NurA family.


FUNCTION: Involved in the biosynthesis of amylovoran which functions as a virulence factor. May be involved in the polymerization or late modification of the repeating units. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: To R.meliloti ExoP.


FUNCTION: Specifically methylates position 8 of adenine 2503 in 23S rRNA. Confers resistance to some classes of antibiotics. FUNCTION: Specifically methylates position 8 of adenine 2503 in 23S rRNA. Confers resistance to some classes of antibiotics, such as chloramphenicol, florfenicol, clindamycin and linezolid. FUNCTION: Specifically methylates position 8 of adenine 2503 in 23S rRNA. Can also methylate position 2 of A2503 after the primary methylation at position 8 is complete, to form 2,8-dimethyladenosine; however, C8 is its preferred target. Confers resistance to several classes of antibiotics such as phenicols, lincosamides, oxazolidinones, pleuromutilins, and streptogramin A. The antibiotic resistance conferred by Cfr is provided by methylation at the 8 position and is independent of methylation at the 2 position of A2503. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. Cfr subfamily. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. Cfr subfamily.


FUNCTION: May play a role in photosystem I and II biogenesis. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbN family.


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


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the tigger transposable element derived protein family.


FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Host endosome membrane; Single-pass type I membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. SIMILARITY: Belongs to the HIV-1 env protein family.


FUNCTION: Specifically methylates the N7 position of guanine in position 535 of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methyltransferase superfamily. RNA methyltransferase RsmG family.


FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.


FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.


FUNCTION: Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrB is probably involved in transfer of electrons from TtrC to TtrA (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.


FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S16 family.


FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate. SIMILARITY: Belongs to the AP endonuclease 2 family.


FUNCTION: Binds the 23S rRNA. SIMILARITY: Belongs to the bacterial ribosomal protein bL31 family. Type A subfamily.


FUNCTION: Sulfur carrier protein which probably makes part of a sulfur- relay system. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sulfur carrier protein TusA family.