FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS19 family.


FUNCTION: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. SUBCELLULAR LOCATION: Host nucleus, host nucleolus Host cytoplasm Secreted Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. SIMILARITY: Belongs to the lentiviruses Tat family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 04 subfamily.


FUNCTION: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium (PubMed:28479320). May be required for ciliary entrance and transport of specific ciliary cargo proteins such as che-3 which are related to motility (PubMed:28479320). Required for normal morphology and function of ciliated amphid sensory neurons (PubMed:16648645, PubMed:7705621). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Cell projection, dendrite Perikaryon Note=Highly expressed in the transition zones between the cilium basal body and the dendrites. SIMILARITY: Belongs to the IFT46 family.


FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to form the UBC2-RAD18 ubiquitin ligase complex involved in postreplicative repair (PRR) of damaged DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RAD18 family.


FUNCTION: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cell membrane; Single-pass type I membrane protein Cell projection, lamellipodium Cell projection, filopodium. SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted. SIMILARITY: Belongs to the SCF family.


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


FUNCTION: Probable electron transporter required for biotin synthase activity. SIMILARITY: Belongs to the flavodoxin family. MioC subfamily.


FUNCTION: Flavin-dependent halogenase involved in the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols. The halogenase catalyzes the transfer of a single chlorine atom to the melleolide backbone, resulting in a 6'-chloromelleolide product. The enzyme acts on free substrate and does not depend on carrier-protein-dependent acceptor molecules. SIMILARITY: Belongs to the flavin-dependent halogenase family.


FUNCTION: Transcription repressor. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Involved in immunity against exogenously supplied nisin. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: To E.coli YibI.


FUNCTION: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.


FUNCTION: Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK. Triggers activation of myeloid cells when associated with TYROBP (PubMed:10604985). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


FUNCTION: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the selenoprotein S family.


FUNCTION: Translocates protons across the thylakoid membrane and transfers electrons from photosystem II to photosystem I. It receives electrons from the Rieske iron-sulfur protein and passes them to plastocyanin. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome f family.


FUNCTION: Proton-coupled monocarboxylate symporter. Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L- lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate (PubMed:9786900, PubMed:32415067). Dimerization is functionally required and both subunits work cooperatively in transporting substrate (PubMed:32415067). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Cytoplasm Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (By similarity). SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MCTS1 family.


FUNCTION: Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. SIMILARITY: Belongs to the PCNA family.


FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL24 family.


FUNCTION: Regulates membrane-cell wall junctions and localized cell wall deposition. Required for establishment of the Casparian strip membrane domain (CSD) and the subsequent formation of Casparian strips, a cell wall modification of the root endodermis that determines an apoplastic barrier between the intraorganismal apoplasm and the extraorganismal apoplasm and prevents lateral diffusion. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Very restricted localization following a belt shape within the plasma membrane which coincides with the position of the Casparian strip membrane domain. SIMILARITY: Belongs to the Casparian strip membrane proteins (CASP) family.


SIMILARITY: Belongs to the phosphoribulokinase family.


FUNCTION: Probable membrane-anchored myosin receptors. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.


FUNCTION: Catalyzes the conversion of fatty acids such as long-chain and very long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity) (PubMed:11112418, PubMed:12975357, PubMed:14516277). Can activate diverse saturated, monosaturated and polyunsaturated fatty acids (PubMed:11112418, PubMed:14516277). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle. Microsome. Endoplasmic reticulum Cell membrane. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily.


FUNCTION: May be involved in plant development processes. SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.


FUNCTION: May be involved in arginine transport. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Note=Exhibits a punctated pattern in the cytoplasm, which partially ovelaps with lysosomes. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.


FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the small GTPase superfamily. Arf family.


SIMILARITY: Belongs to the ninF family.


FUNCTION: Required for complex colony architecture. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.


FUNCTION: Involved in the regulation of anaerobiotic glycerol metabolism. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Citrate synthase-like protein; part of the gene cluster that mediates the biosynthesis of oryzines, natural products with an unusual maleidride backbone (PubMed:30104550). The two subunits of the fungal fatty acid synthase oryfasA and oryfasB probably form octenoic acid (Probable). This fatty acid is most likely activated by the acyl-CoA ligase oryP to give octenyl-CoA before the citrate synthase-like protein oryE catalyzes condensation with oxaloacetate to form tricarboxylic acid (Probable). The next steps of the pathways are conjectural, but a favorite possible route has been proposed, beginning with decarboxylation and concomitant dehydration by the decarboxylase oryM, followed by tautomerization, which may lead to the production of a diene intermediate (Probable). Reduction of this diene intermediate could give the known metabolite piliformic acid (Probable). On the pathway to oryzine B and oryzine A, however, hydroxylation of the diene by the alpha-ketoglutarate-dependent dioxygenase oryG and lactonisation by the lactonohydrolases oryH or oryL could give oryzine B directly (Probable). Finally, enoyl reduction by the dehydrogenase oryD would then convert oryzine B into oryzine A (Probable). SIMILARITY: Belongs to the citrate synthase family.


FUNCTION: Fumarylacetoacetase involved in the tyrosine degradation pathway. SIMILARITY: Belongs to the FAH family.


FUNCTION: Single-stranded RNA-binding protein. SIMILARITY: Belongs to the orbivirus non-structural protein NS2 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0295 family.


FUNCTION: Deaminates adenosine-34 to inosine in many tRNAs. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family. ADAT2 subfamily.


FUNCTION: DNA-binding protein that regulates the transcription of several genes and is involved in heart development and limb pattern formation. Binds to the core DNA motif of NPPA promoter. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the cytoplasm and the nucleus. Acetylation at Lys-338 promotes nuclear retention.


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


FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family.


FUNCTION: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Can sense membrane curvature and has in vitro vesicle- to-membrane remodeling activity. Involved in retrograde endosome-to-TGN transport of lysosomal enzyme receptors (IGF2R, M6PR and SORT1). Plays a role in targeting ligand-activated EGFR to the lysosomes for degradation after endocytosis from the cell surface and release from the Golgi. Involvement in retromer-independent endocytic trafficking of P2RY1 and lysosomal degradation of protease-activated receptor-1/F2R. Promotes KALRN- and RHOG-dependent but retromer-independent membrane remodeling such as lamellipodium formation; the function is dependent on GEF activity of KALRN. Required for endocytosis of DRD5 upon agonist stimulation but not for basal receptor trafficking (By similarity). SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans- Golgi network membrane; Peripheral membrane protein; Cytoplasmic side Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium Note=Enriched on tubular elements of the early endosome membrane. Binds preferentially to highly curved membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Colocalized with SORT1 to tubular endosomal membrane structures called endosome-to-TGN transport carriers (ETCs) which are budding from early endosome vacuoles just before maturing into late endosome vacuoles. Colocalized with F-actin at the leading edge of lamellipodia in a KALRN-dependent manner. SIMILARITY: Belongs to the sorting nexin family.


FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifically exchanges the top DNA strands. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerC subfamily.


FUNCTION: Transcriptional repressor of xylose-utilizing enzymes. SIMILARITY: Belongs to the ROK (NagC/XylR) family.


FUNCTION: E3 ubiquitin ligase that plays a role in several processes including innate antiviral immnity, cell migration and chemotaxis. Acts as a 'Lys-63'-specific ubiquitin ligase for MAPK1/ERK2 and MAPK3/ERK1, promoting their activation by facilitating their interaction with MAP2K1 and MAP2K2. Plays also a role in cell migration and chemotaxis by acting as a stable focal adhesion component upon recruitment by multi-adapter protein paxillin/PXN. Functions in the RIGI-mediated interferon induction pathway upstream or at the level of MAVS. Inhibits NF-kappa-B activation by turnover of 'Lys-63'-linked ubiquitination of MAP3K7/TAK1. Mechanistically, prevents TRIM8 cytoplasmic translocation and thus inhibits TRIM8-mediated 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 in the cytoplasm. Plays also an important regulatory effect on the activation of hepatic stellate cells (HSCs). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell junction, focal adhesion Note=Localizes to focal adhesions during the early stage of adhesion biogenesis. SIMILARITY: Belongs to the TRIM/RBCC family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL32 family.


FUNCTION: Peptidoglycan hydrolase involved in the splitting of the septum during cell division. Binds to both alpha and beta-chains of human fibrinogen as well as fibronectin, which suggests a role in the colonization of host factor-coated material or host tissue. Also exhibits lytic activity against S.carnosus and S.aureus cells but not against M.luteus cells. FUNCTION: Peptidoglycan hydrolase involved in the splitting of the septum during cell division. Binds to both alpha and beta-chains of human fibrinogen as well as fibronectin, which suggests a role in the colonization of host factor-coated material or host tissue. Also exhibits lytic activity against S.carnosus and S.aureus cells but not against M.luteus cells. FUNCTION: Peptidoglycan hydrolase involved in the splitting of the septum during cell division. SUBCELLULAR LOCATION: Secreted Cell surface. SUBCELLULAR LOCATION: Secreted Cell surface. SUBCELLULAR LOCATION: Secreted Cell surface.


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.


SIMILARITY: Belongs to the MvhD/VhuD family.


FUNCTION: Plays a role in the inhibition of the host innate immune response. Mechanistically, promotes the autophagy-mediated lysosomal degradation of host TBK1 and affects IRF3 nuclear translocation to block type I IFN production. SUBCELLULAR LOCATION: Virion Host cytoplasm. SIMILARITY: Belongs to the asfivirus A137R family.


FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for limb and craniofacial development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.


SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.


FUNCTION: [Irisin]: May mediate beneficial effects of muscular exercise. SUBCELLULAR LOCATION: [Irisin]: Secreted Note=Detected in the blood of individuals subjected to endurance exercise. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Peroxisome membrane; Single-pass type I membrane protein.


FUNCTION: Counteracts the host Pycsar antiviral defense system. Phosphodiesterase that enables metal-dependent hydrolysis of host cyclic nucleotide Pycsar defense signals such as cCMP and cUMP. SIMILARITY: Belongs to the anti-Pycsar protein Apyc1 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Plasminogen subfamily.


SIMILARITY: Belongs to the leguminous lectin family.


FUNCTION: Probably part of the ABC transporter complex YxeMNO that could be involved in amino-acid import. May transport S-methylcysteine. Probably responsible for the translocation of the substrate across the membrane (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family.


SIMILARITY: Belongs to the G-alpha family.


FUNCTION: Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family.


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


FUNCTION: Antimicrobial peptide active against a variety of Gram- positive bacterial strains but not against Gram-negative bacteria. Has weak antifungal activity against a slime mold isolate. Has weak hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily.


FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.


FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. SUBCELLULAR LOCATION: Cytoplasm Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.


FUNCTION: Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CPA3 antiporters (TC 2.A.63) subunit B family.


FUNCTION: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.


FUNCTION: Probably involved in membrane protein trafficking at the base of the ciliary organelle. May function in cilia biogenesis. Isoform 2 is required for proper retinal function and organization. SUBCELLULAR LOCATION: Cell projection, cilium membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body. SIMILARITY: Belongs to the small GTPase superfamily. Arf family.


FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Membrane, caveola. SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin subfamily.


FUNCTION: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpA family.


FUNCTION: Probably linked to the pathogenesis of listerial infection. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family.


FUNCTION: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase- dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non- LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.


FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily.


SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the asparaginase 1 family.


SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein.


FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID, and the RNA polymerase II associated general transcription factor complex TFIIF. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, facilitation of DNA opening and initiation of transcription. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA- TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit has stimulatory activity. Component of the SWI/SNF complex, an ATP- dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the TAF14 family.


FUNCTION: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the CCR4/nocturin family.


FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Essential component of cell cytoskeleton; plays an important role in cytoplasmic streaming, cell shape determination, cell division, organelle movement and extension growth. This is considered as one of the reproductive actins. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family.


FUNCTION: Calcium-dependent N-acyltransferase involved in the biosynthesis of N-acyl ethanolamines (NAEs) in the brain (PubMed:27399000). Transfers the sn-1 fatty acyl chain of phosphatidylcholine (fatty acyl donor) to the amine group of phosphatidylethanolamine (fatty acyl acceptor) to generate N-acyl phosphatidylethanolamine (NAPE). Similarly can use plasmenylethanolamine as a fatty acyl acceptor to form N-acyl plasmenylethanolamine (N-Acyl-PlsEt). Both NAPE and N-Acyl-PlsEt can serve as precursors of bioactive NAEs like N-arachidonoyl phosphatidylethanolamine also called anandamide (PubMed:27399000, PubMed:29447909). Has weak phospholipase A2 and lysophospholipase activities (PubMed:27399000, PubMed:15866882). Regulates intracellular membrane trafficking that requires modulation of membrane curvature as it occurs by enrichment in lysophospholipids. Promotes tubule formation involved in clathrin-independent endocytotic trafficking and cargo recycling (PubMed:24413173). SUBCELLULAR LOCATION: Cytoplasm, cytosol Early endosome membrane; Peripheral membrane protein; Cytoplasmic side Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Targeted to clathrin-independent endocytotic vesicles through binding to phosphoinositides, especially phosphatidylinositol 4,5-bisphosphates.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the adenylyl cyclase class-3 family.


FUNCTION: With S5 and S12 plays an important role in translational accuracy. 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. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS4 family.


FUNCTION: Required to modulate lifespan, in concert with hcf-1, acting redundantly with 14-3-3-like protein ftt-2. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the 14-3-3 family.


FUNCTION: Transcription factor that binds to the promoter and the enhancer regions of target genes. Binds to the enhancer element PRE-I (positive regulatory element-I) of the IL-4 gene (PubMed:7665092). Binds to the promoter and the enhancer of the immunoglobulin heavy chain. Binds to GPE1, a cis-acting element in the G-CSF gene promoter. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.


FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. FUNCTION: Catalyzes the phospholipid dependent N-acylation of the N- terminal cysteine of apolipoprotein, the last step in lipoprotein maturation. FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo- inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM). FUNCTION: Transfers mannose from GDP-mannose to lipid acceptors (works best on C20-C95 lipid monophosphate substrates in which the lipid can be modified, tested with the C-terminal domain expressed in M.smegmatis) to form polyprenol monophosphomannose (PPM). PMM is an alkai-stable sugar donor which adds mannose-phosphate residues to triacylated-phosphatidyl-myo-inositol mannosides (PIM2), eventually leading to generation of the cell wall glycolipid lipoglycan modulins lipoarabinomannan (LAM) and lipomannan (LM). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: In the C-terminal section; belongs to the glycosyltransferase 2 family. SIMILARITY: In the N-terminal section; belongs to the CN hydrolase family. Apolipoprotein N-acyltransferase subfamily.


FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus. SIMILARITY: Belongs to the RRP4 family.


FUNCTION: Seed storage protein. Might be integrated via inter-chain disulfide bonds within the glutenin polymer (By similarity). SIMILARITY: Belongs to the prolamin family.


FUNCTION: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells (PubMed:25302411). The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues (PubMed:25302411). One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine (PubMed:25302411). After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT (PubMed:25302411). In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as tailoring enzymes to produce the intermediate dechloroaspirochlorine (PubMed:25302411). Ultimately, chlorination of dechloroaspirochlorine by the halogenase aclH is the last step in the aspirochlorine pathway (PubMed:25302411). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.


FUNCTION: Necessary for efficient adipogenesis. Does not show ion channel activity. SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM120 family.


FUNCTION: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by catalyzing both the hydration and the hydrolysis of 3-(methylthio)acryloyl-CoA (MTA-CoA) to acetaldehyde, CO2, MeSH, and CoA (PubMed:21562561, PubMed:23704947). SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


FUNCTION: Binds with low affinity to muscular (alpha-1-beta-1-delta- epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Orphan group II sub-subfamily.


FUNCTION: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: In the N-terminal section; belongs to the leguminous lectin family. SIMILARITY: In the C-terminal section; belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Catalyzes reversively the conversion of L-aspartate beta- semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination with L-glutamate. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11- dehydrocorticosterone to corticosterone in the presence of NADP(H) (PubMed:17470521). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes (By similarity). Plays a role in the secretion of aqueous humor in the eye, maintaining a normotensive, intraocular environment (By similarity). Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids (By similarity). It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates. Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7- oxopregnenolone and 7beta-hydroxypregnenolone, 7- oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en- 17-one), among others (By similarity). Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7- oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite (By similarity). 7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation (By similarity). Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism (By similarity). Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation. Binds phosphatidylinositol 3-phosphate (PtdIns3P). Activated by the STK11/AMPK signaling pathway upon starvation, WDR45 is involved in autophagosome assembly downstream of WIPI2, regulating the size of forming autophagosomes. Together with WIPI1, promotes ATG2 (ATG2A or ATG2B)-mediated lipid transfer by enhancing ATG2-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes. Probably recruited to membranes through its PtdIns3P activity. SUBCELLULAR LOCATION: Preautophagosomal structure Cytoplasm Note=Diffusely localized in the cytoplasm under nutrient-rich conditions. Localizes to autophagic structures during starvation-induced autophagy. SIMILARITY: Belongs to the WD repeat PROPPIN family.


FUNCTION: Hydroxynaphthalene reductase-like protein; part of the Pks2 gene cluster that mediates the formation of infectious structures (appressoria), enabling these fungi to kill insects faster (PubMed:29958281). The product of the Pks2 gene cluster is different from the one of Pks1 and has still not been identified (PubMed:29958281). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Polymerizes D(-)-3-hydroxybutyryl-CoA to create PHB which consists of thousands of hydroxybutyrate molecules linked end to end. PHB serves as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PHA/PHB synthase family. Type I PhaC subfamily.


FUNCTION: Cytochrome P450 of the CYP74A subfamily involved in the biosynthesis of jasmonic acid from lipoxygenase-derived hydroperoxides of free fatty acids. Catalyzes the synthesis of unstable allene oxide, which is further converted spontaneously by hydrolysis or cyclization. Can use 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic acid (13- HPOT) and 13S-hydroperoxy-9(Z),11(E)-octadecadienoic acid (13-HPOD) as substrates. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (PubMed:21441247, PubMed:23406870). Also involved in the regulation of axon outgrowth and synaptogenesis (By similarity). The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity). SUBCELLULAR LOCATION: Synapse Golgi apparatus Presynapse Cytoplasmic vesicle, secretory vesicle, synaptic vesicle Note=Dissociates from synaptic vesicles and redistributes into the axon during action potential firing, in a step that precedes fusion of vesicles with the plasma membrane. Reclusters to presynapses after the cessation of synaptic activity. SIMILARITY: Belongs to the synapsin family.


FUNCTION: Heterodimer CA-CB: Crotoxin is a potent presynaptic neurotoxin that possesses phospholipase A2 (PLA2) activity and exerts a lethal action by blocking neuromuscular transmission (PubMed:8513799). It consists of a non-covalent association of a basic and weakly toxic PLA2 subunit (CBa2, CBb, CBc, or CBd), with a small acidic, non- enzymatic and non-toxic subunit (CA1, CA2, CA3 or CA4) (PubMed:8513799). The complex acts by binding to a specific 48-kDa protein (R48) receptor located on presynaptic membranes, forming a transient ternary complex CA-CB-R48, followed by dissociation of the CA-CB complex and release of the CA subunit (PubMed:12657321). At equilibrium, only the CB subunits remain associated with the specific crotoxin receptor (PubMed:12657321). In addition to neurotoxicity, crotoxin has been found to exert myotoxicity, nephrotoxicity, and cardiovascular toxicity (By similarity). Moreover, anti-inflammatory, immunomodulatory, anti-tumor and analgesic effects of crotoxin have also been reported (By similarity). FUNCTION: Monomer CBd: The basic subunit of crotoxin is a snake venom phospholipase A2 (PLA2) that exhibits weak neurotoxicity (10-fold less than the heterodimer) and very strong anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (By similarity). In addition, it shows the same effects described for the heterodimer and binds the nucleotide-binding domain (NBD1) of CFTR chloride channels and increases the channel current (By similarity). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (PubMed:8513799). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.


FUNCTION: Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis. SUBCELLULAR LOCATION: Endosome, multivesicular body membrane; Peripheral membrane protein Prevacuolar compartment membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein. SIMILARITY: Belongs to the MON1/SAND family.


FUNCTION: Cooperates with CIITA to promote transcription of MHC class I and MHC class II genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ZXD family.


FUNCTION: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N- glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.


FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex, thereby playing a role in RNA- mediated gene silencing (RNAi) by miRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARS2 family.


FUNCTION: May participate in DNA packaging/capsid maturation events. Promotes efficient incorporation of tegument proteins UL46, UL49, and US3 into virions. May also play a role in capsid transport to the trans-Golgi network (TGN) (By similarity). SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus. SIMILARITY: Belongs to the alphaherpesvirinae UL21 protein family.


FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.


FUNCTION: Maximin-H5 shows antibacterial activity only against the Gram-positive bacteria S.aureus. The other bacterial and fungal strains tested were resistant to it. The presence of metal ions, like Zn(2+) and Mg(2+), did not increase its antimicrobial potency. Does not show hemolytic activity (in a concentration up to 80 uM). FUNCTION: Maximin-3 shows antibacterial activity against both Gram- positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. It possess a significant cytotoxicity against tumor cell lines. It possess a significant anti- HIV activity. It shows high spermicidal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family.


FUNCTION: Required for bipolar spindle formation. May act as a regulator of the p34cdc2/cyclin B kinase. Required for full activation of the plo1 kinase. However, in cut12.1 cells at restrictive temperature the H1 kinase does rise concomitant with entry into mitosis, indicating that cut12 is not required for activation of p34cdc2/cyclin B. The cut12.s11 allele may promote cdc2-independent phosphorylation of SPB proteins thereby overcoming the requirement for cdc25 in cell cycle progression. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.


FUNCTION: Interacts with ToxR and stimulates its activity. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein; Periplasmic side.


FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4. May play a role in regulation of cell division in renal glomeruli. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3.


FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. Inhibits also the host cGAS/STING-mediated type I interferon production by inducing host IRF3 degradation through the proteasome pathway. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the asfivirus MGF 360 family.


FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C- terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8- phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATG3 family.


FUNCTION: Required for cell expansion in leaves. May mediate brassinosteroid (BR)-induced leaf growth. May play a role in the control of BR responses in roots. May be involved in signaling processes that coordinate BR responses with environmental or developmental signals. SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the EXORDIUM family.


FUNCTION: Plays an important role in the resistance of F.nucleatum to the antibacterial agent 3-chloro-DL-alanine (3CA), thanks to its 3CA chloride-lyase (deaminating) activity. FUNCTION: Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia; methanethiol (methyl mercaptan) is considered to be one of the main causes of the oral malodor associated with periodontitis. Also displays homocysteine desulfhydrase activity, degrading homocysteine to produce hydrogen sulfide, 2-oxobutanoate and ammonia. L-cysteine and S-methyl-L-cysteine are poor substrates for the enzyme. SIMILARITY: Belongs to the trans-sulfuration enzymes family. L- methionine gamma-lyase subfamily.


SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to 5'-pGpG (PubMed:18344366, PubMed:19376848). Cannot use cyclic AMP or cyclic GMP (PubMed:18344366). Part of the RocSAR two-component regulatory signaling system (also known as the SadARS system), which regulates biofilm maturation, type III secretion and expression of the cup fimbrial-gene cluster (PubMed:15687209, PubMed:15659157). Negatively regulates the expression of cup genes by antagonizing the activity of RocA1 (PubMed:15659157).


FUNCTION: Essential for the synthesis of the polyglutamate capsule of B.anthracis which is one of the principal virulence factors during anthrax infection. May form a polyglutamyl synthetase complex together with proteins CapB and CapC. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CapA family.


SIMILARITY: Belongs to the lymphocryptovirus BTRF1 family.


FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity. Ubiquitinates MAGED1 antigen leading to its subsequent degradation by proteasome (By similarity). May be involved in protein sorting.


FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. May have a carrier function to deliver PLP to the target enzymes or a protective function so that PLP does not inactivate essential lysines in proteins (PubMed:26872910). Does not have amino acid racemase activity (PubMed:24097949). SIMILARITY: Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family. SIMILARITY: Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.


FUNCTION: Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type 2 tetrahydrodipicolinate N- succinyltransferase family.


FUNCTION: Regulates the transcription of several operons and genes involved in the biogenesis of Fe-S clusters and Fe-S-containing proteins.


FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex cfd1-nbp35. Electrons are transferred to dre2 from NADPH via the FAD- and FMN-containing protein tah18. Tah18-dre2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit rnr2. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space. SIMILARITY: Belongs to the anamorsin family.


FUNCTION: Required for correct meiotic chromosome segregation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.


FUNCTION: DNA nicking enzyme that cleaves extruded cruciform DNA at its tip. Probably nicks viral hairpins. SUBCELLULAR LOCATION: Virion. Note=Virion core. SIMILARITY: Belongs to the orthopoxvirus OPG042 family.


FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis. SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.


FUNCTION: Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1. SIMILARITY: Belongs to the peptidase C19 family.


FUNCTION: D-mannose/D-glucose-binding lectin. SIMILARITY: Belongs to the leguminous lectin family.


FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein. FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family. SIMILARITY: Belongs to the DsbB family.


FUNCTION: Intercellular signaling molecule that inhibits excision of the mobile genetic element ICEBs1 when cells are crowded by cells that contain ICEBs1 and produce the PhrI peptide (PubMed:16105942). Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Acts by inhibiting RapI activity (PubMed:16105942). SUBCELLULAR LOCATION: Secreted Cytoplasm Note=Produced through an export-import maturation process. SIMILARITY: Belongs to the Phr family.


FUNCTION: Involved in the regulation of plant growth.


FUNCTION: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (By similarity). Plays an important role in hepatic triglyceride metabolism (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.


FUNCTION: Involved in parasite invasion of erythrocytes. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the apicomplexan parasites AMA1 family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS7 family.


FUNCTION: Plays a role in the inhibition of host apoptosis by sequestering and inactivating several proapoptotic BCL-2 proteins, including BAK1 and BAX. Prevents the conformational activation of both of them. SUBCELLULAR LOCATION: Host mitochondrion Host membrane; Single-pass membrane protein.


FUNCTION: May be involved in the regulation of the production of pyocyanine, one of the major virulence factors secreted by P.aeruginosa, and other virulence factors. SIMILARITY: Belongs to the con-10 family.


FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacteria in soy sauce brewing (PubMed:30466366). Might be required for efficient secretion of heptelidic acid (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: High-affinity permease involved in the transport of the cationic amino acids (e.g. arginine, and, to a lower extent, citrulline and glutamate). Transport mostly basic amino acids, and, to a lower extent neutral and acidic amino acids. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.


FUNCTION: With TAX4, acts as a positive regulator of INP51 activity and phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates signaling through the cell integrity pathway, including the MAP kinase SLT2. Seems also to be involved in rDNA silencing. SIMILARITY: Belongs to the IRS4 family.


FUNCTION: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria (PubMed:24231807, PubMed:26774479, PubMed:27099988). Required to bridge the calcium-sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU (PubMed:24231807). Plays a central role in regulating the uniplex complex response to intracellular calcium signaling (PubMed:27099988). Acts by mediating activation of MCU and retention of MICU1 to the MCU pore, in order to ensure tight regulation of the uniplex complex and appropriate responses to intracellular calcium signaling (PubMed:27099988). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein Note=MAIP1 is required to assist sorting of EMRE/SMDT1 into mitochondrion by protecting EMRE/SMDT1 against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB) (PubMed:27642048). SIMILARITY: Belongs to the SMDT1/EMRE family.


FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). The Cas4 region acts as a ssDNA exonuclease, while the Cas1 region acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette (By similarity). SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated exonuclease Cas4 family. SIMILARITY: In the C-terminal section; belongs to the CRISPR-associated endonuclease Cas1 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the vasopressin/oxytocin family.


FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks alpha-3-beta-2/CHRNA3-CHRNB2 (IC(50)=11 nM), alpha- 7/CHRNA7 (IC(50)=27.1-59 nM (rat)/ 290 nM (human)), alpha-3-beta- 4/CHRNA3-CHRNB4 (IC(50)=160 nM), and alpha-6/alpha-3-beta-2-beta-3 (CHRNA6/CHRNA3-CHRNB2-CHRNB3) (IC(50)=201 nM) nAChR (PubMed:16803900, PubMed:30025921, PubMed:34955864). In the OmIA-AChBP complex, this toxin occupies all five binding pockets located between two adjacent subunits of the homopentamer (PubMed:34955864). Despite a competitive binding mode observed in the co-crystal structure, it displays functional insurmountable antagonism at alpha-7 and alpha-3-beta-4 nAChRs (PubMed:34955864). It also shows biphasic-inhibition at alpha-7 nAChRs in the presence of the positive allosteric modulator PNU120596, with a preference for the high-affinity binding site following prolonged exposure (PubMed:34955864). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily.


FUNCTION: Required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. ATG14 mediates the specific binding of the VPS34 PI3-kinase complex I to the preautophagosomal structure (PAS) (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Note=TRS85 is required for the recruitment of ATG14 to the PAS. SIMILARITY: Belongs to the ATG14 family.


FUNCTION: Molecular chaperone that interact with a ClpP-like protease involved in degradation of denatured proteins in the chloroplast (PubMed:21737456). The ATPase activity of CLPD is stimulated by CLPT1 (PubMed:25149061). Has no ADPase activity (PubMed:21737456). Interacts with transit peptides with a positional preference (PubMed:21737456, PubMed:22545953). Localization of the signal sequence at the N-terminal end of a protein seems mandatory for interaction to take place (PubMed:22545953). SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the ClpA/ClpB family. ClpD subfamily.


FUNCTION: Has a broad spectrum of activity against both Gram-positive and Gram-negative bacteria and S.cerevisiae. Has insecticidal and hemolytic activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Medium-length antimicrobial peptide (group 3) family. Ponericin-W subfamily.


FUNCTION: Functions with the transcription factor TfAP-2 to regulate octopamine neuronal signaling pathways that control behaviors such as male aggression, male mating, and the initiation of feeding (PubMed:30231996, PubMed:24142897, PubMed:25187989). Required for TfAP- 2 transcriptional activity in octopaminergic neurons (PubMed:24142897, PubMed:25187989). Functions with TfAP-2 to regulate expression of genes which are involved in promoting octopamine production and secretion from octopaminergic neurons, such as Tbh and Vmat (PubMed:24142897, PubMed:25187989). Octopamine then modulates feeding and male aggression by regulating the expression of the satiation hormone Dsk in insulin- producing cells (IPCs) (PubMed:24142897, PubMed:25187989). Functions with octopamine and Dsk as part of a negative feedback loop to prevent overeating; acts with TfAP-2 to regulate octopamine signaling pathways that initiate feeding, then octopamine activates expression of Dsk which inhibits consummatory behavior (PubMed:25187989). May also be involved in negatively regulating nociception in larvae to prevent spontaneous pain and hyperalgesia (PubMed:30231996).


SUBCELLULAR LOCATION: Mitochondrion intermembrane space Note=Imported into the mitochondria via the mitochondrial disulfide relay system. SIMILARITY: Belongs to the CMC4 family.


FUNCTION: Its interaction with CUL3 suggests that it may act as a substrate adapter in some E3 ligase complex (By similarity). Does not affect the function of Kv channel Kv2.1/KCNB1, Kv1.2/KCNA2, Kv4.2/KCND2 and Kv3.4/KCNC4 (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Nucleus Note=Predominantly cytoplasmic, translocated to the nucleus upon interaction with Rep proteins.


FUNCTION: Viral mimic of EIF2S1/eIF-2alpha that acts as a pseudosubstrate for EIF2AK2/PKR kinase (PubMed:8099586, PubMed:9199350). Inhibits therefore EIF2S1/eIF-2alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff (PubMed:8099586, PubMed:9199350). Determinant of host species specificity (PubMed:32056708). SIMILARITY: Belongs to the poxviridae K3 protein family.


FUNCTION: Member of the two-component regulatory system HptS/HptR that regulates genes involved in hexose phosphate transport system in response to changes in extracellular phosphate sources. Activates uhpT expression to facilitate glucose-6-phosphate/G6P utilization by directly binding to its promoter. Antagonizes CcpA-dependent transcription of a subset of CcpA-regulated genes involved in antibiotic susceptibility. SUBCELLULAR LOCATION: Cytoplasm.


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


FUNCTION: Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine. FUNCTION: Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side- chain amino group of a substrate lysine. SIMILARITY: Belongs to the Pup ligase/Pup deamidase family. Pup- conjugating enzyme subfamily.


FUNCTION: Part of an ATP-driven transport system. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 9 family. Lipoprotein receptor antigen (Lrai) subfamily.


FUNCTION: Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH. SIMILARITY: Belongs to the peptidase C1 family.


FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA). SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Involved in both the arginine and lysine biosynthetic pathways. Phosphorylates the LysW-bound precursors glutamate (for arginine biosynthesis), respectively alpha-aminoadipate (for lysine biosynthesis). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetylglutamate kinase family. LysZ subfamily.


FUNCTION: Catalyzes the reversible decarboxylation of 4- hydroxybenzoate. SIMILARITY: Belongs to the UbiD family.


SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


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


FUNCTION: Regulator of deubiquitinating complexes. Activates deubiquitination by increasing the catalytic turnover without increasing the affinity of deubiquitinating enzymes for the substrate (By similarity). SIMILARITY: Belongs to the WD repeat WDR48 family.


FUNCTION: Multifunctional protein that includes general (non sugar- specific) and sugar-specific components of the phosphoenolpyruvate- dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FrwABC PTS system is involved in fructose transport. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PEP-utilizing enzyme family.


SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca Note=Found in the postacrosomal region of the perinuclear theca.


FUNCTION: Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway. SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvT family. CAF17 subfamily.


FUNCTION: Acts as an osmosensitive calcium-permeable cation channel (By similarity). Mechanosensitive ion channel that converts mechanical stimuli into a flow of ion (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.


FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity). SIMILARITY: Belongs to the eIF-1A family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TMEM144 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the expansin family. Expansin-like A subfamily.


FUNCTION: Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O- acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the influenza viruses hemagglutinin family.


FUNCTION: Minor structural protein present in one or two copies per virion. Does not seem to play a role in capsid assembly, but is essential for production of infectious virus (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the vesivirus VP2 protein family.


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


FUNCTION: Required for centrosome duplication and formation and function of the mitotic spindle. Essential for the development of the cerebral cortex. May regulate the production of neurons by controlling the orientation of the mitotic spindle during division of cortical neuronal progenitors of the proliferative ventricular zone of the brain. Orientation of the division plane perpendicular to the layers of the cortex gives rise to two proliferative neuronal progenitors whereas parallel orientation of the division plane yields one proliferative neuronal progenitor and a post-mitotic neuron. A premature shift towards a neuronal fate within the progenitor population may result in an overall reduction in the final number of neurons and an increase in the number of neurons in the deeper layers of the cortex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Note=Localizes to the interphase and S phase centrosome. During mitosis, partially associated with the mitotic spindle. Concentrates at the plus ends of microtubules coincident with kinetochores in metaphase and anaphase in a CENPF-dependent manner. Also localizes to the cleavage furrow during cytokinesis. manner. Also localizes to the cleavage furrow during cytokinesis. SIMILARITY: Belongs to the nudE family.


FUNCTION: Zinc finger transcription factor which acts as both a transcriptional activator and repressor (PubMed:23911329, PubMed:30956009). Binds to the promoters of genes that contain the 5'- CTTATCA-3' DNA consensus sequence in their regulatory region (PubMed:23911329, PubMed:31532389). Functions downstream of the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:23911329, PubMed:27401555). Involved in normal development, lifespan, stress response, lipid metabolism, innate immunity and exit from the developmentally arrested larval state known as dauer (PubMed:23911329, PubMed:27401555, PubMed:29949773, PubMed:31532389, PubMed:33009389). Required for stress-induced expression of hsp-90 and resistance to heat stress, perhaps as part of a systemic stress signaling pathway (PubMed:29949773). Involved in maintenance of proteostasis (PubMed:29949773). Under hypoxic stress increases lipid levels by positively regulating fatty acid synthesis via fat-7 expression (PubMed:33009389). Associates with homeobox protein ceh-60 at the promoters of some stress-responsive genes to regulate expression; may require phosphorylation for transcriptional repression activity (PubMed:30956009). Acts downstream of nhr-14 to activate transcription of intestinal metal transporter smf-3, modulating innate immunity and iron uptake (PubMed:31532389). May act downstream of the mTORC2 signaling mediated pathway (PubMed:27401555). May act in a mutually exclusive manner with the FOXO transcription factor daf-16 (PubMed:23911329, PubMed:27401555). SUBCELLULAR LOCATION: Chromosome Nucleus Cytoplasm Note=Nuclear localization under normal conditions, cytoplasmic as a result of heat-stress (PubMed:23911329). Nuclear localization declines over normal lifespan (PubMed:23911329). Exposure to Gram-negative bacterium P.aeruginosa enhances nuclear localization (PubMed:31532389). Hypoxic stress enhances nuclear localization (PubMed:33009389). SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


SIMILARITY: Belongs to the LEA type 2 family.


FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). FUNCTION: The transmembrane protein (TM) 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 viral and target cell membrane fusion, 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane; Single-pass type I membrane protein Host cell 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. SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral 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 (By similarity).


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaA Na(+)/H(+) (TC 2.A.33) antiporter family.


FUNCTION: Snake venom phospholipase A2 (PLA2) that impairs hemostasis. It weakly inhibits ADP-induced platelet aggregation when tested on platelet rich plasma from human and rabbit blood (15-25% of inhibition at 5-10 ug of enzyme), and dose-dependently inhibits blood coagulation, possibly by inhibiting thrombin activation. Exhibits high hydrolytic activities toward L-dipalmitoyl phosphatidylcholine. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn- phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.


FUNCTION: May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. FUNCTION: May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation. SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily. SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily.


FUNCTION: Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complexes, to modulate their activities. Recognizes the host NF-kappa-B regulator BTRC through the presence of a DSGXS motif in the C-terminal substrate recognition domain. SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton. SIMILARITY: Belongs to the rotavirus NSP1 family.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNURF family.


FUNCTION: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes (PubMed:21778237). Down-regulates activation of NF- kappa-B. Inhibits TNF-induced NFKB1 activation. SUBCELLULAR LOCATION: Nucleus Cytoplasm.


FUNCTION: Secreted immune-induced peptide induced by Toll signaling (PubMed:9736738). Has a role in resistance to bacterial and fungal infections (PubMed:25915418, PubMed:29920489). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bomanin family.


FUNCTION: Effector protein involved in non-host recognition. SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion system (TTSS).


FUNCTION: Blocks Kv11/ERG potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily.


FUNCTION: May play an essential role in neuronal pathway recognition and ventral muscle attachment site selection. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family.


FUNCTION: Part of the RFC clamp loader complex which loads the PCNA sliding clamp onto DNA. The complex possesses DNA-dependent ATPase activity which is further stimulated by PCNA. In conjunction with PCNA stimulates DNA synthesis by PolB, relieving inhibition by replication protein A (RPA). SIMILARITY: Belongs to the activator 1 small subunits family. RfcS subfamily.


SIMILARITY: Belongs to the PhzF family.


FUNCTION: Component of the Integrator complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'- box-dependent processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA- metabolizing metallo-beta-lactamase-like family. INTS9 subfamily.


FUNCTION: Required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Constitutes the ATP-driven core of the motor and binds the precursor preprotein (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the heat shock protein 70 family.


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


FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'- terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down- regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA. SUBCELLULAR LOCATION: [DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]: Mitochondrion. Note=Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress (By similarity). The cleaved APEX2 is only detected in mitochondria. SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus Nucleus speckle Endoplasmic reticulum Cytoplasm. Note=Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA- irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1- dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 63-79). S-nitrosylation at Cys-92 and Cys-309 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. Detected in the cytoplasm of B-cells stimulated to switch (By similarity). SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.


FUNCTION: Cleaves internal linkages in 1,3-beta-glucan. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the glycosyl hydrolase 81 family.


FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 17 (Hntx-9) subfamily.


FUNCTION: Capsid protein that self-assembles to form the pseudo- hexameric capsomers of the icosahedral capsid (By similarity). The capsid is constructed of 2760 pseudo-hexameric capsomers and 12 pentameric capsomers, with a T=277 symmetry, about 200 nm in diameter (By similarity). The capsid encapsulates the DNA-containing nucleoid, the core shell and the inner membrane (By similarity). Plays an essential role in virion assembly (By similarity). Involved in virus attachment to the host cell (By similarity). SUBCELLULAR LOCATION: Virion Host endoplasmic reticulum membrane; Peripheral membrane protein Host cytoplasm, host cytosol Note=Present in the outer part of the capsid shell (By similarity). Localizes to the viral factory at 16 hpi (By similarity). SIMILARITY: Belongs to the NCLDV major capsid protein family.


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). Cas3 plus Cascade participate in CRISPR interference, the third stage of CRISPR immunity. Functions as a ssDNA-dependent ATPase; dsDNA, ssRNA do not stimulate ATPase activity, while other nucleotides (aside from dATP) are not hydrolyzed. Functions as a ssDNA nuclease; activity does not require ATP. Functions as an ATP-dependent helicase; helicase activity requires hydrolysable ATP. Unwinds both DNA/DNA hybrids and RNA/DNA hybrids, moving mostly in a 3' to 5' direction. SIMILARITY: In the central section; belongs to the CRISPR-associated helicase Cas3 family. SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated nuclease Cas3-HD family.


FUNCTION: Catalyzes the addition of Glc, the second sugar moiety of the O56-antigen repeating unit, to GlcNAc-pyrophosphate-undecaprenol. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the glycosyltransferase 2 family.


SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CHK2 subfamily.


FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)- containing RNAs, and regulates their stability. M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing. Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT and ribonuclease P/MRP complexes, depending on the context. The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation. M6A-containing mRNAs containing a binding site for RIDA/HRSP12 (5'-GGUUC-3') are preferentially degraded by endoribonucleolytic cleavage: cooperative binding of RIDA/HRSP12 and YTHDF2 to transcripts leads to recruitment of the ribonuclease P/MRP complex. Other m6A-containing mRNAs undergo deadenylation via direct interaction between YTHDF2 and CNOT1, leading to recruitment of the CCR4-NOT and subsequent deadenylation of m6A- containing mRNAs (By similarity). Required maternally to regulate oocyte maturation: probably acts by binding to m6A-containing mRNAs, thereby regulating maternal transcript dosage during oocyte maturation, which is essential for the competence of oocytes to sustain early zygotic development. Also required during spermatogenesis: regulates spermagonial adhesion by promoting degradation of m6A-containing transcripts coding for matrix metallopeptidases (By similarity). Also involved in hematopoietic stem cells specification by binding to m6A- containing mRNAs, leading to promote their degradation (By similarity). Also acts as a regulator of neural development by promoting m6A- dependent degradation of neural development-related mRNA targets (By similarity). Inhibits neural specification of induced pluripotent stem cells by binding to methylated neural-specific mRNAs and promoting their degradation, thereby restraining neural differentiation. Regulates circadian regulation of hepatic lipid metabolism: acts by promoting m6A-dependent degradation of PPARA transcripts. Regulates the innate immune response to infection by inhibiting the type I interferon response: acts by binding to m6A-containing IFNB transcripts and promoting their degradation. May also act as a promoter of cap- independent mRNA translation following heat shock stress: upon stress, relocalizes to the nucleus and specifically binds mRNAs with some m6A methylation mark at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby promoting cap-independent mRNA translation. Regulates mitotic entry by promoting the phase-specific m6A-dependent degradation of WEE1 transcripts. Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation. The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules. May also recognize and bind RNAs modified by C5-methylcytosine (m5C) and act as a regulator of rRNA processing (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, P-body Cytoplasm, Stress granule Nucleus Note=Localizes to the cytosol and relocates to the nucleus following heat shock stress. Can partition into different structures: into P- bodies in unstressed cells, and into stress granules during stress. SIMILARITY: Belongs to the YTHDF family. YTHDF2 subfamily.


SIMILARITY: Belongs to the asfivirus helicase C962R family.


FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H2A family.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O- acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Part of an actin-like archaeal cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Forms cell-spanning helical structures. Colocalizes with crenactin.