FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Golgi apparatus Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. SIMILARITY: Belongs to the prion family.


FUNCTION: Polysaccharide lyase that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. Acts specifically on alginate and each of its block structures, with highest activity toward poly-beta-D-mannuronate (poly-ManA). Shows an exolytic mode of action, producing unsaturated monomers. Displays a very low activity against poly-beta-D-glucuronate (poly-GlcA), and is not active on poly- alpha-D-galacturonate, hyaluronan, heparin, heparan sulfate and chondroitin sulfate. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the polysaccharide lyase 17 family.


FUNCTION: Master transcriptional regulator of the unfolded protein response (UPR) that recognizes and binds to the UPR element (UPRE) in the promoter of UPR-regulated genes (PubMed:19132084, PubMed:22028661, PubMed:21217201). In the canonical UPR pathway, the ireA RNase splices the cytoplasmic mRNA hacA, which alters the reading frame to allow translation of the bZIP transcription factor hacA (PubMed:19132084, PubMed:33087521). Induces the expression of pmrA, scrA and spfA in response to UPR (PubMed:32487759, PubMed:34663092). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 38 family.


FUNCTION: Not known. Encoded on a subgenomic RNA (RNA3) synthesized during replication and which is co-terminal with RNA1.


FUNCTION: Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP plays a dual role in early-stage biofilm development and host cell recognition. Positively regulates the expression of the ecp operon (By similarity). FUNCTION: Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP is found in both commensal and pathogenic strains and plays a dual role in early-stage biofilm development and host cell recognition. Positively regulates the expression of the ecp operon (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the EcpR/MatA family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. PFL subfamily.


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


SIMILARITY: Belongs to the CFAP97 family.


FUNCTION: Has antimicrobial activity, but no hemolytic activity. Preference on killing Gram-negative non-enteric bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bombinin family.


FUNCTION: Required for induction of expression of the formate dehydrogenase H and hydrogenase-3 structural genes.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL23 family.


FUNCTION: Probably functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the importin beta family. Importin beta-2 subfamily.


FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5- androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid. SIMILARITY: Belongs to the GST superfamily. Alpha family.


FUNCTION: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory. Plays a role in regulating urinary Ca(2+) and Na(+) excretion. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Perikaryon Cell projection, dendrite Cell projection, dendritic spine. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC8 subfamily.


FUNCTION: Essential helicase. SIMILARITY: Belongs to the helicase family. UvrD subfamily.


FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. FUNCTION: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Bacterial flagellum basal body. SIMILARITY: Belongs to the FlgH family. SIMILARITY: Belongs to the FlgH family.


FUNCTION: Host defense peptide that exhibits antimicrobial activity against both Gram-negative bacteria, such as E.coli and S.typhimurium, and Gram-positive bacteria, such as S.aureus and B.subtilis (By similarity). Inhibits cell adhesion of E.coli on intestinal epithelial enterocytes (By similarity). Causes rapid permeabilization of both the outer and inner membrane of E.coli, leading to morphological alterations on the bacterial surface (By similarity). Binds to bacterial lipopolysaccharides (LPS) with high affinity, and may thereby be involved in immunoregulation through LPS neutralization (By similarity). May contribute to epididymal innate immunity and protect the sperm against attack by microorganisms (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: May contribute to neddylation of cullin components of SCF- type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity).


SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the bacterial glucokinase family.


FUNCTION: High-affinity transporter for external inorganic phosphate. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. phosphate:H(+) symporter (TC 2.A.1.9) family.


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


FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'- triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase family. SIMILARITY: In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.


FUNCTION: Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides. SIMILARITY: Belongs to the transferase hexapeptide repeat family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily.


FUNCTION: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB). SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the STAM family.


FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase. SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.


FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IMPDH/GMPR family.


FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF- beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Cell membrane Membrane raft Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.


FUNCTION: Regulates lateral organ growth. Functionally redundant with NGA1, NGA2 and NGA4. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Intradiol ring-cleavage dioxygenase involved in an alternative pathway to the protocatechuic acid pathway since it is active on hydroxyquinol and catechol but not on protocatechuic acid. SIMILARITY: Belongs to the intradiol ring-cleavage dioxygenase family.


FUNCTION: Involved in the maintenance of Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and Golgi. Involved in hormone-induced steroid biosynthesis in testicular Leydig cells. Recruits PI4KB to the Golgi apparatus membrane; enhances the enzyme activity of PI4KB activity via its membrane recruitment thereby increasing the local concentration of the substrate in the vicinity of the kinase. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion Note=Also mitochondrial (via its interaction with PBR).


FUNCTION: Component of the cuticle of the pupa of Tenebrio molitor.


SIMILARITY: Belongs to the universal ribosomal protein uS17 family.


FUNCTION: Either a functional dehydrogenase or a non-functional fragment. SIMILARITY: Belongs to the DadA oxidoreductase family.


FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLU7 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. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.


FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus (By similarity). SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm. SUBCELLULAR LOCATION: [Isoform P4]: Host nucleus. SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm. SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus. SIMILARITY: Belongs to the lyssavirus protein P family.


FUNCTION: Probable transcription factor involved in the control of specification of mesoderm and endoderm. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family.


FUNCTION: Serine protease inhibitor that inhibits trypsin (Ki=50 nM) and probably also chymotrypsin (Kd=1.6 nM). Has an anti-inflammatory effect in LPS-activated macrophages in vitro, specifically reducing release of TNF and IL6 but not nitric oxide and reducing expression of IL1B precursor. FUNCTION: Dual-function toxin that inhibits both serine proteases and voltage-gated potassium channels (PubMed:26404319, PubMed:33158163). Has potent activity on both trypsin (Ki=50 nM) and chymotrypsin (Kd=1.6 nM) (PubMed:26404319). Shows inhibitory activity against 5 of the 7 potassium channels tested (rKv1.1/KCNA1; IC(50)=12.6, hKv1.2/KCNA2; IC(50)=181.7, hKv1.3/KCNA3; IC(50)=29.7, rKv1.6/KCNA6; IC(50)=43.9, drosophila Shaker; IC(50)=114.9) (PubMed:33158163). Has an anti- inflammatory effect in LPS-activated macrophages in vitro, specifically reducing release of TNF and IL6 but not nitric oxide and reducing expression of IL1B precursor (PubMed:26404319). In contrast to some paralogs, this protein decreases reactive oxygen species (ROS) level in the oxidative stress agent 6-hydroxydopamine (6-OHDA)-induced neurotoxicity model, but does not show cytoprotective activity on neuroblastoma cells (PubMed:33802055). This protein also shows a weak free-radical scavenging activity (PubMed:33802055). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily.


FUNCTION: Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases. RNA replication depends on the availability of soluble nucleoprotein. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Localizes in cytoplasmic inclusion bodies. SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.


FUNCTION: Transcription factor which acts as both an activator and a repressor (By similarity). Activates transcription of a number of genes including the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 which are involved in protection against oxidative stress (By similarity). Required for normal brain development (PubMed:34723967). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region Note=Localizes to the nucleus and cytoplasm with higher levels in the nucleus where it is expressed in a diffuse manner (PubMed:34723967). Located in the cytoplasm of spermatocytes and strongly accumulates at the perinuclear region in elongated spermatids (PubMed:25609838).


FUNCTION: Ribosome biogenesis factor. May be required for both optimal rDNA transcription and pre-rRNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus.


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


FUNCTION: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. May regulate microtubule organization at least in part by targeting the microtubule severing protein KATNA1 to the centrosome. Also positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus ends. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the centripetal motion of secretory vesicles and the coupling of the nucleus and centrosome. Also required during brain development for the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Plays a role, together with DISC1, in the regulation of neurite outgrowth. Required for mitosis in some cell types but appears to be dispensible for mitosis in cortical neuronal progenitors, which instead requires NDE1. Facilitates the polymerization of neurofilaments from the individual subunits NEFH and NEFL. Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome, centromere, kinetochore Cytoplasm, cytoskeleton, spindle Note=Localizes to the interphase centrosome and the mitotic spindle. Localizes to the cell body of the motor neurons and colocalizes with assembled neurofilaments within axonal processes. Localizes to the microtubules of the manchette in elongated spermatids. Colocalizes with DISC1 in the perinuclear region, including the centrosome. Localizes to the kinetochore in a CENPF- dependent manner (By similarity). SIMILARITY: Belongs to the nudE family.


FUNCTION: Component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Involved in resistance to acriflavine, and required for normal growth on a range of sole carbon sources, including fructose, cellobiose, raffinose, and starch, and reduced utilization of amino acids, including GABA and beta-alanine, as sole carbon and nitrogen sources (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acrB family.


FUNCTION: Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release- activated Ca(2+) (CRAC) channel subunit ORAI1. Involved in enamel formation. Activated following interaction with STIMATE, leading to promote STIM1 conformational switch. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single- pass type I membrane protein Sarcoplasmic reticulum Cytoplasm, cytoskeleton Note=Translocates from the endoplasmic reticulum to the cell membrane in response to a depletion of intracellular Ca(2+) and is detected at punctae corresponding to junctions between the endoplasmic reticulum and the cell membrane. Associated with the microtubule network at the growing distal tip of microtubules. Colocalizes with ORAI1 at the cell membrane. Colocalizes preferentially with CASQ1 at endoplasmic reticulum in response to a depletion of intracellular calcium (By similarity).


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


FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.


FUNCTION: Regulates actin polymerization by inhibiting the actin- nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors. Participates in an incoherent feedforward loop at the lamellipodium tip where it inhibits the ARP2/2 complex in response to Rac signaling and where Rac also stimulates actin polymerization through the WAVE complex. Involved in steering cell migration by controlling its directional persistence (By similarity). SUBCELLULAR LOCATION: Cell projection, lamellipodium Note=Colocalized with the WAVE complex at lamelliupodium tip. SIMILARITY: Belongs to the Arpin family.


FUNCTION: 4'-O-methyltransferase converting norbelladine to 4'-O- methylnorbelladine (By similarity). 4'-O-methylnorbelladine is a precursor to all Amaryllidaceae alkaloids such as galanthamine, lycorine and haemanthamine, and including haemanthamine- and crinamine- type alkaloids, promising anticancer agents (By similarity). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.


FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5- phosphate, a key step in isoprenoid and cholesterol biosynthesis (PubMed:9325256, PubMed:18302342, PubMed:9392419, PubMed:11278915). SUBCELLULAR LOCATION: Cytoplasm Peroxisome. SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase subfamily.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D- manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the protein kinase superfamily. KdkA/RfaP family.


FUNCTION: Putative RNA-binding protein. May be involved in regulating gene expression during embryonic development. Seems to be involved in endoderm formation. Ectopic expression results in endoderm formation in the absence of mesoderm induction. SIMILARITY: Belongs to the BicC family.


FUNCTION: Receptor for the attractant L-serine and related amino acids. FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family.


FUNCTION: May be involved in endocytic processes and/or other transport pathways mediated by vesicle trafficking. May interact functionally with ROP protein. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Ras family.


SIMILARITY: Belongs to the agmatine deiminase family.


FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid including cleroda-dienols, and peregrinol lactones and furan derivatives, dopaminergic diterpenoids that can bind to dopamine receptors in the human pituitary gland, have probably ability to lower prolactin levels, and are used to treat menstrual cycle disorders (e.g. premenstrual syndrome and mastodynia) (Probable). Terpene synthase that produces kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP) (PubMed:29315936). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Transcription factor that binds preferentially to a variant of the octamer motif (5'-ATGATAAT-3'). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the POU transcription factor family. Class-6 subfamily.


SIMILARITY: Belongs to the ModE family.


FUNCTION: NAD(+) hydrolase (NADase) that cleaves NAD(+) into nicotinamide and 3' cyclic ADP-D-ribose (3'cADPR, v2-cADPR) (PubMed:34657283, PubMed:36048923). Upon infiltration of A.thaliana with this bacteria an effector-triggered immunity-like phenotype (ETI- like, cell death with severe chlorosis) is seen, 3'cADPR levels rise while NAD(+) levels remain constant. Plant immune responses are suppressed. Triggers hypersensitive response-like cell death in Nicotiana tabacum cv. Xanthi and N.benthamiana when transiently expressed, depletes NAD(+) in N.benthamiana. Causes cell death upon induction in yeast due to NAD(+) depletion and/or 3'cADPR itself (PubMed:34657283). Transgenic A.thaliana expressing HopAM1 suppresses its plant immune system upon challenge; the plants produce 3'cADPR without significantly depleting NAD(+) (PubMed:36048923). SUBCELLULAR LOCATION: Host cytoplasm Host cytoplasm, host cytosol Note=Delivered into plants by a type III secretion system (T3SS).


FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.


FUNCTION: Galbeta1-3GalNAcbeta1-4Galbeta1-4Glc oligosaccharide-binding lectin. Binds strongly to the oligosaccharides of ganglioside GM1b and to a lesser extent its precursor asialo-GM1 (PubMed:31769916, PubMed:33328520). Binds weakly to asialo-GM2 oligosaccharide and to the glycan moiety of globo-series stage-specific embryonal antigen 4 (SSEA- 4) hexaose (PubMed:31769916). Binds galactose, N-acetylgalactose and lactose. Does not bind GM1 (PubMed:33328520). Does not bind to Gal- beta1,3-GalNAc (Thomsen-Friedenreich antigen), the oligosaccharide of GM1a ganglioside or SSEA-4 tetraose. Does not bind to N-glycans, O- glycans or glycosaminoglycans of glycoproteins. Does not bind Lewis glycans, derivatives of lactose or N-acetyllactosamine or blood group (ABH-type) oligosaccharides (PubMed:31769916). Does not bind glucose (PubMed:33328520). Has hemagglutination activity towards rabbit erythrocytes (PubMed:31769916, PubMed:33328520). Displays cytotoxic effects against various cultured cell lines including human breast (MCF-7), cervical (HeLa) and colon cancer (Caco2) cell lines, as well as dog kidney (MDCK) cell line that express asialo-GM1 oligosaccharide at their cell surface. Shows dose- and time-dependent activation of MKK3/6, ERK1/2 and p38 MAPK, as well as caspase-3/9 in HeLa cervical cancer cells. No cytotoxic effect on BT474 human breast cancer cell line. May be involved in recognition of glycans found on parasitic or symbiotic microorganisms (PubMed:31769916).


FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has ssRNase activity. Upon expression in E.coli inhibits growth in liquid culture; this toxic effect is neutralized by coexpression with cognate antitoxin VapB1. Its RNase activity is partially inhibited in vitro by VapB1 (PubMed:22046301). SIMILARITY: Belongs to the PINc/VapC protein family.


SUBCELLULAR LOCATION: Mitochondrion intermembrane space. SIMILARITY: Belongs to the CHCHD7 family.


FUNCTION: Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HAM1 NTPase family.


FUNCTION: Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA (By similarity). SIMILARITY: Belongs to the FlgM family.


FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.


FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: The heterotrimeric Elba complex is required for chromatin domain boundary function during early embryogenesis. It binds to a 8-bp sequence 5'-CCAATAAG-3' in the Fab-7 insulator or boundary element in the bithorax complex and contributes to its insulator or boundary activity (PubMed:23240086). Elba2 can act as a transcriptional repressor and binds the palindromic sequence 5'-CCAATTGG-3' to mediate transcriptional repression (PubMed:25561495). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Tegument protein that can bind to various RNA transcripts. Plays a role in the attenuation of selective viral and cellular mRNA degradation by modulating the activity of host shutoff RNase UL41/VHS. Also plays a role in the primary envelopement of virions in the perinuclear space, probably by interacting with two nuclear egress proteins UL31 and UL34. SUBCELLULAR LOCATION: Virion tegument Host nucleus Host cytoplasm Note=Major tegument protein of the virion. Undergoes nucleocytoplasmic shuttling during infection. Localizes to the major sites of transcription in the infected cell nucleus. SIMILARITY: Belongs to the alphaherpesvirinae HHV-1 UL47 family.


FUNCTION: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to nutrient stress (By similarity). Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (By similarity). Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity). SUBCELLULAR LOCATION: Cytoplasm Peroxisome Cytoplasmic granule Note=Localizes to cytoplasmic granules in the presence of BLMH. SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.


FUNCTION: Plays an essential role in viral DNA replication. May generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs. SIMILARITY: Belongs to the baculoviridae LEF-1 family.


FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:8020965). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure (PubMed:8020965). Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, axon. SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily.


SIMILARITY: Belongs to the SXP/RAL-2 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family. SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.


FUNCTION: Probable xylan acetyltransferase required for 2-O- and 3-O- monoacetylation of xylosyl residues in xylan (PubMed:29569182). Possesses extremely low activity in vitro (PubMed:29569182). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.


FUNCTION: Carrier protein involved in proton-driven auxin influx. May mediate the formation of auxin gradient from developing leaves (site of auxin biosynthesis) to tips (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family. Amino acid/auxin permease (AAAP) (TC 2.A.18.1) subfamily.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Neurotoxin that blocks voltage-independent calcium-activated potassium channels (KCNN1=SK1, KCNN2=SK2, KCNN3=SK3). SUBCELLULAR LOCATION: Secreted.


FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance.


FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Appears to be colocalized with SLC4A1. SIMILARITY: Belongs to the glycophorin A family.


FUNCTION: Transcription factor involved in regulation of RNA polymerase II-dependent transcription. Also involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells (By similarity). SUBCELLULAR LOCATION: Nucleus Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL67 family.


FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system. Part of the plasmid-stabilizing activity of plasmid R1; when R1 is lost cells die rapidly. When overexpressed kills cells within 5 minutes; causes collapse of the transmembrane potential and arrest of respiration (PubMed:3019679). Its toxic effect is partially neutralized by antisense RNA Sok. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Hok/Gef family.


FUNCTION: Chaperone involved in the maturation of iron-sulfur [Fe-S] cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HSCB and ISU1 (PubMed:19865480). In cooperation with other chaperones, Hsp70s are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions (Probable). SUBCELLULAR LOCATION: Mitochondrion Cytoplasm, cytosol. SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33) family. DnaK subfamily.


FUNCTION: The outer wall protein binds to the middle cell wall protein. SUBCELLULAR LOCATION: Secreted, cell wall, S-layer. Note=This bacterium is covered by a S-layer with hexagonal symmetry.


FUNCTION: This protein is essential for plasmid replication; it is involved in copy control functions. SIMILARITY: Belongs to the IncFII RepA family.


FUNCTION: Putative odorant or sperm cell receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and CHLH. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent chelation step (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.


FUNCTION: Gastrointestinal hormone and neuropeptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NPY family.


FUNCTION: May play a role in p53/TP53-mediated apoptosis. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Regulates phosphorylation of a number of proteins involved in translation regulation including EIF2A, EIF4EBP1 and RPS6KB1. May be involved in the endoplasmic reticulum stress response (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Lipid-anchor. SIMILARITY: Belongs to the Niban family.


FUNCTION: Suppresses apoptosis in host cell to promote the viral replication (By similarity). Has the ability to potentially bind to all the members of the proapoptotic Bcl-2 family (By similarity). Inhibits autophagy by interacting with host Beclin 1 (BECN1) (By similarity). SUBCELLULAR LOCATION: Host mitochondrion Host endoplasmic reticulum. SIMILARITY: Belongs to the Bcl-2 family.


FUNCTION: May be involved in hydrogen uptake for the reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is likely to be the physiological electron carrier for the enzyme. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:30468448). Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti- cancer drugs highly active against colon cancer cells (PubMed:30468448). Hydroxylates germacrene A acid to 6-alpha-hydroxy- germacrne A acid, a precursor of sesquiterpene lactones that spontaneously undergoes a lactonization which yields costunolide (PubMed:21515683). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.


FUNCTION: Possesses strong antiplasmodial activity against the intra- erythrocyte stage of P.falciparum in vitro. IC(50) for inhibiting P.falciparum growth is 1.15 uM. Specifically interacts with infected erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. Has neither antibacterial nor antifungal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 36 family. 02 subfamily.


FUNCTION: May regulate the transcription of the frlABCDR operon, involved in the utilization of fructoselysine and psicoselysine.


FUNCTION: Tubulin-binding protein involved in microtubule formation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the phosducin family.


FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Chromosome. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. SIMILARITY: Belongs to the pescadillo family.


FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL10, CXCL11 and CXCL13. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding- competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus Secreted Note=Translocates to nuclear foci during heat shock. SIMILARITY: Belongs to the small heat shock protein (HSP20) family.


FUNCTION: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing (PubMed:24038582, PubMed:24916387, PubMed:27050523, PubMed:30844405, PubMed:31358901, PubMed:34160127). Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules (PubMed:24038582, PubMed:24916387, PubMed:30844405). Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10 (PubMed:34160127). Also involved in the alternative splicing of several genes including TJP1. Binds the pre- mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs (PubMed:31358901, PubMed:27050523). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RRM RBM47 family.


FUNCTION: Transports acetate. Also able to transport glycolate. FUNCTION: Transports acetate. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family. SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21) family.


FUNCTION: Probably acts as a transcriptional activator and may be involved in disease resistance pathways (By similarity). Binds to the GCC-box pathogenesis-related promoter element. Involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways mediated by ethylene, that seems to depend on a protein kinase cascade and to be influenced by methyl- jasmonate. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ethylene-response factor family. Class 1 subfamily.


FUNCTION: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbZ family.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids without apparent head group selectivity (By similarity). Contributes to phospholipid remodeling of low-density lipoprotein (LDL) and high- density lipoprotein (HDL) particles. Hydrolyzes LDL phospholipids releasing unsaturated fatty acids that regulate macrophage differentiation toward foam cells (By similarity). May act in an autocrine and paracrine manner. Secreted by immature mast cells, acts on nearby fibroblasts upstream to PTDGS to synthesize prostaglandin D2 (PGD2), which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity). Secreted by epididymal epithelium, acts on immature sperm cells within the duct, modulating the degree of unsaturation of the fatty acyl components of phosphatidylcholines required for acrosome assembly and sperm cell motility. Facilitates the replacement of fatty acyl chains in phosphatidylcholines in sperm membranes from omega-6 and omega-9 to omega-3 polyunsaturated fatty acids (PUFAs). Coupled to lipoxygenase pathway, may process omega-6 PUFAs to generate oxygenated lipid mediators in the male reproductive tract (By similarity). At pericentrosomal preciliary compartment, negatively regulates ciliogenesis likely by regulating endocytotic recycling of ciliary membrane protein (By similarity). Coupled to cyclooxygenase pathway provides arachidonate to generate prostaglandin E2 (PGE2), a potent immunomodulatory lipid in inflammation and tumorigenesis (By similarity). At colonic epithelial barrier, preferentially hydrolyzes phospholipids having arachidonate and docosahexaenoate at sn-2 position, contributing to the generation of oxygenated metabolites involved in colonic stem cell homeostasis (By similarity). Releases C16:0 and C18:0 lysophosphatidylcholine subclasses from neuron plasma membranes and promotes neurite outgrowth and neuron survival (By similarity). SUBCELLULAR LOCATION: Secreted Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Recycling endosome Note=Localized at pericentrosomal preciliary compartment. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Negatively regulates the expression of the gbsAB and opuB operons. Required to control expression of these genes in response to choline availability. Also required to down-regulate glycine betaine production once cellular adjustment to high osmolarity has been achieved. SIMILARITY: Belongs to the GbsR family.


FUNCTION: Involved in the transposition of the insertion sequence IS2.


FUNCTION: Probable secreted effector that translocates into the nuclei of host cells to reprogram the expression of targeted genes by binding on effector binding elements in rice. SUBCELLULAR LOCATION: Secreted Host nucleus.


FUNCTION: pEKW and poly-His-poly-Gly peptides may serve as metalloproteinase inhibitors during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the prey. FUNCTION: [C-type natriuretic peptide]: Exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3). SUBCELLULAR LOCATION: Secreted. SIMILARITY: In the C-terminal section; belongs to the natriuretic peptide family. SIMILARITY: In the central section; belongs to the pHpG family.


FUNCTION: Envelope protein required for virus entry into host cell and for cell-cell fusion (syncytium formation). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the intracellular mature virion (IMV) membrane. SIMILARITY: Belongs to the poxviridae A28 protein family.


FUNCTION: Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the FliT family.


FUNCTION: A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain. SUBCELLULAR LOCATION: Cell membrane.


FUNCTION: Plays an important role in the removal of damaged mitochondria via mitophagy by controlling the stability and localization of RAB7A (By similarity). Required for the recruitment of RAB7A and ATG9A vesicles to damaged mitochondria and promotes the stability of RAB7A by inhibiting its proteasomal degradation during mitophagy (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the RIMOC1 family.


FUNCTION: Myoactive peptide. Increases the amplitude and frequency of spontaneous contractions and tonus of hindgut muscle. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Monoheme cytochrome which is the immediate electron donor to P840 of the photosynthetic reaction center complex. FUNCTION: Monoheme cytochrome which is the immediate electron donor to P840 of the photosynthetic reaction center complex. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.


FUNCTION: Serine/threonine protein kinase that specifically phosphorylates chloroplast precursor proteins in the cytosol within the cleavable presequences (transit peptides). May be part of a cytosolic regulatory network involved in chloroplast protein import. Does not phosphorylate mitochondrion precursor proteins. Specific for ATP and does not utilize other NTPs (PubMed:17090544, PubMed:16429265). Plays a role in chloroplast biogenesis and differentiation in cotyledons, possibly through phosphorylation of chloroplast preproteins (PubMed:21799034). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Binds to the brush border membrane vesicles of scarab larvae and damages the gut wall somehow to allow the vegetative cells of P.popilliae to enter the hemolymph. SIMILARITY: Belongs to the delta endotoxin family.


FUNCTION: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation (By similarity). Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of maternal mRNAs in immature oocytes, inhibiting their translation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule. SIMILARITY: Belongs to the ZAR1 family.


FUNCTION: Phosphorylates mevalonate 3-phosphate to form mevalonate 3,5- bisphosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5- phosphate.


FUNCTION: Fatty acid conjugase converting 18:2(9Z, 12Z) to calendic acid 18:3(8E, 10E, 12Z) (PubMed:11067856). Converts alpha-linolenic acid (18:3(9Z, 12Z, 15Z)) into 18:4(8E, 10E, 12Z, 15Z) (PubMed:11067856). Also has weak activity on the mono-unsaturates 16:1(9Z) and 18:1(9Z) producing two conjugated double bonds at delta(8) and delta(10) position (By similarity). SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family.


FUNCTION: Inositol phosphate kinase with a broad substrate specificity (PubMed:12027805, PubMed:12223481, PubMed:28882892, PubMed:30420721, PubMed:30624931). Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) first to inositol 1,3,4,5-tetrakisphosphate and then to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) (PubMed:12027805, PubMed:12223481, PubMed:28882892, PubMed:30624931). Phosphorylates inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) (PubMed:12223481). Phosphorylates glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate to glycero-3-phospho-1D-myo-inositol 3,4,5- trisphosphate (PubMed:30420721, PubMed:28882892). Plays an important role in MLKL-mediated necroptosis via its role in the biosynthesis of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Binding of these highly phosphorylated inositol phosphates to MLKL mediates the release of an N-terminal auto-inhibitory region, leading to activation of the kinase. Essential for activated phospho- MLKL to oligomerize and localize to the cell membrane during necroptosis (PubMed:29883610). Required for normal embryonic development, probably via its role in the biosynthesis of inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) and inositol hexakisphosphate (InsP6) (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.


FUNCTION: This protein appears to play an important role in virus penetration at the level of cell fusion. The N-terminal proximal region is essential for fusion ability. Essential in fusing the outermost of the two Golgi-derived membranes enveloping the virus with the plasma membrane, and in its subsequent release extracellularly. SUBCELLULAR LOCATION: Virion membrane. Note=Envelope fraction of virions. SIMILARITY: Belongs to the poxviruses fusion protein family.


FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Required for autophagy (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Note=Peripheral membrane protein of pre-autophagosomal structure (PAS) and vacuole. SIMILARITY: Belongs to the WD repeat PROPPIN family.


FUNCTION: Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4 subfamily.


FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein (PubMed:19692335). Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon.


FUNCTION: Transcriptional repressor that contribute to growth arrest during terminal macrophage differentiation by repressing target genes involved in Ras-dependent proliferation. Represses MMP1 promoter activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family.


FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed:10759893, PubMed:11897662, PubMed:12842904, PubMed:14718166, PubMed:15664198, PubMed:16151251, PubMed:21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed:11897662, PubMed:14718166, PubMed:15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed:29478807). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol (PubMed:21454524, PubMed:29408485). Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit (PubMed:15621527). FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. May also cooperate with HIRA to promote replication-independent chromatin assembly. SUBCELLULAR LOCATION: Nucleus Chromosome. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ASF1 family.


FUNCTION: [Envelope glycoprotein E1]: Forms a heterodimer with envelope glycoprotein E2, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and ApoE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan- 1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR- SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). FUNCTION: [Mature core protein]: Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN- alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity). FUNCTION: [Envelope glycoprotein E2]: Forms a heterodimer with envelope glycoprotein E1, which mediates virus attachment to the host cell, virion internalization through clathrin-dependent endocytosis and fusion with host membrane (By similarity). Fusion with the host cell is most likely mediated by both E1 and E2, through conformational rearrangements of the heterodimer required for fusion rather than a classical class II fusion mechanism (By similarity). The interaction between envelope glycoprotein E2 and host apolipoprotein E/APOE allows the proper assembly, maturation and infectivity of the viral particles (By similarity). This interaction is probably promoted via the up- regulation of cellular autophagy by the virus (By similarity). E1/E2 heterodimer binds host apolipoproteins such as APOB and APOE thereby forming a lipo-viro-particle (LVP) (By similarity). APOE associated to the LVP allows the initial virus attachment to cell surface receptors such as the heparan sulfate proteoglycans (HSPGs), syndecan-1 (SDC1), syndecan-1 (SDC2), the low-density lipoprotein receptor (LDLR) and scavenger receptor class B type I (SCARB1) (By similarity). The cholesterol transfer activity of SCARB1 allows E2 exposure and binding of E2 to SCARB1 and the tetraspanin CD81 (By similarity). E1/E2 heterodimer binding on CD81 activates the epithelial growth factor receptor (EGFR) signaling pathway (By similarity). Diffusion of the complex E1-E2-EGFR-SCARB1-CD81 to the cell lateral membrane allows further interaction with Claudin 1 (CLDN1) and occludin (OCLN) to finally trigger HCV entry (By similarity). Inhibits host EIF2AK2/PKR activation, preventing the establishment of an antiviral state (By similarity). Viral ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on liver sinusoidal endothelial cells and macrophage-like cells of lymph node sinuses (By similarity). These interactions allow the capture of circulating HCV particles by these cells and subsequent facilitated transmission to permissive cells such as hepatocytes and lymphocyte subpopulations (By similarity). SUBCELLULAR LOCATION: [Envelope glycoprotein E2]: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single-pass type I membrane protein Host lipid droplet Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). SUBCELLULAR LOCATION: [Mature core protein]: Virion Host cytoplasm Host nucleus Host lipid droplet Note=Only a minor proportion of core protein is present in the nucleus (By similarity). Probably present on the surface of lipid droplets (By similarity). SUBCELLULAR LOCATION: [Envelope glycoprotein E1]: Virion membrane; Single-pass type I membrane protein Host endoplasmic reticulum membrane; Single-pass type I membrane protein Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase (By similarity). After cleavage, the membrane sequence is retained at the C-terminus of the protein, serving as ER membrane anchor (By similarity). A reorientation of the second hydrophobic stretch occurs after cleavage producing a single reoriented transmembrane domain (By similarity). These events explain the final topology of the protein (By similarity). SUBCELLULAR LOCATION: [Core protein precursor]: Host endoplasmic reticulum membrane; Single-pass membrane protein Host mitochondrion membrane; Single-pass type I membrane protein Note=The C-terminal transmembrane domain of the core protein precursor contains an ER signal leading the nascent polyprotein to the ER membrane. SIMILARITY: Belongs to the hepacivirus polyprotein family.


FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Microsome membrane; Peripheral membrane protein Mitochondrion inner membrane; Peripheral membrane protein Note=Post-translationally targeted to mitochondria. TOMM70 is required for the translocation across the mitochondrial outer membrane. After translocation into the matrix, associates with the inner membrane as a membrane extrinsic protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the tyrosinase family. Hemocyanin subfamily.


FUNCTION: May protect the nitrogenase Fe-Mo protein from oxidative damage. SIMILARITY: Belongs to the NifW family.


FUNCTION: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscS (TC 1.A.23) family.


FUNCTION: Acts as a chaperone (By similarity). Might have a role in the infectious process. FUNCTION: Acts as a chaperone. SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the heat shock protein 70 family. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: A bifunctional beta-xylosidase/alpha-L-arabinosidase, exo- enzyme that acts synergistically with endohydrolases. Releases xylose and arabinose from cell walls (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the glycoside hydrolase 3 family.


FUNCTION: Part of the ABC transporter complex AraNPQ involved in the uptake of arabinooligosaccharides (By similarity). AraN captures the substrate and delivers it to the two transmembrane components (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.


FUNCTION: Involved in D-xylose catabolism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the xylose isomerase family.


FUNCTION: Iron transport multicopper ferroxidase required for Fe(2+) ion high affinity uptake. Required to oxidize Fe(2+) to Fe(3+), which is then transported into the cell via the ferric iron permease FTR1. Essential component of copper-dependent iron transport. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein; Extracellular side. SIMILARITY: Belongs to the multicopper oxidase family.


FUNCTION: Vacuolar serine-type carboxypeptidase involved in vacuolar zymogen activation, breakdown of the autophagic body, and autophagosome-dependent protein synthesis (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates (PubMed:19897216). SUBCELLULAR LOCATION: Vacuole lumen Note=The vacuolar sorting receptor VPS10 is required for the delivery of ATG42 to the vacuole lumen. SIMILARITY: Belongs to the peptidase S10 family.


FUNCTION: Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Associated with two foci at the outer edges of the nucleoid region in young cells, and at four foci within both cell halves in older cells. SIMILARITY: Belongs to the ScpA family.


FUNCTION: May sustain the structure of the postsynaptic density (PSD). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein.


FUNCTION: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TAF10 family.


FUNCTION: Appears to be proteolytically inactive. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase A1 family.


FUNCTION: Transcriptional repressor. MXI1 binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional activity by competing for MAX. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: V region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). SUBCELLULAR LOCATION: Cell membrane.


FUNCTION: Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.


FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind inositol tetrakisphosphate (IP4).


FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-methionine (SAM) into adenosine and L-methionine (PubMed:18720493, PubMed:19739191). Is likely stereoselective, specifically hydrolyzing (R)-S-adenosyl-L- methionine ((R)-SAM), the inactive form of the ubiquitous cofactor SAM, and not the active form of SAM, (S)-S-adenosyl-L-methionine (By similarity). Probaly plays a role in preventing accumulation of (R)-S- adenosyl-L-methionine in cells; maintenance of (S)-S-denosyl-L- methionine homochirality is important for cellular health given that the (R)-form is largely inactive as a methyl donor and can function as an inhibitor of methyltransferases (By similarity). Shows very slow iodinase activity in vitro (PubMed:18720493). SIMILARITY: Belongs to the SAM hydrolase / SAM-dependent halogenase family.


FUNCTION: Involved in the biosynthesis of alanine. Catalyzes the transamination of pyruvate by glutamate, leading to the formation of L- alanine and 2-oxoglutarate. Is also able to catalyze the reverse reaction. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Palmitoyltransferase that targets several endosomal SNAREs. Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic end of their transmembrane domain. May have a role in the cellular quality control of transmembrane domain-containing proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. SWF1 subfamily.


FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). FUNCTION: Bradykinin-potentiating peptide both inhibits the activity of the angiotensin-converting enzyme (ACE) and enhances the action of bradykinin by inhibiting the peptidases that inactivate it. It acts as an indirect hypotensive agent. Synthetic Cdt1a, Cdt1b and the short hexapeptide Cdt3 are able to potentiate the hypotensive effect mediated by Bk on the blood pressure of anesthetized rats. SUBCELLULAR LOCATION: Secreted. SIMILARITY: In the N-terminal section; belongs to the bradykinin- potentiating peptide family. SIMILARITY: In the C-terminal section; belongs to the natriuretic peptide family.


FUNCTION: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. SIMILARITY: Belongs to the LplA family.


FUNCTION: [Protein hedgehog N-product]: The dually lipidated hedgehog protein N-product is a morphogen which is essential for a variety of patterning events during development (PubMed:25639794, PubMed:27195754, PubMed:8166882, PubMed:1394430, PubMed:1340474, PubMed:11319862). Establishes the anterior-posterior axis of the embryonic segments and patterns the larval imaginal disks. Binds to the patched (ptc) receptor, which functions in association with smoothened (smo), to activate the transcription of target genes wingless (wg), decapentaplegic (dpp) and ptc. In the absence of hh, ptc represses the constitutive signaling activity of smo through fused (fu). Essential component of a signaling pathway which regulates the Duox-dependent gut immune response to bacterial uracil; required to activate Cad99C- dependent endosome formation, norpA-dependent Ca2+ mobilization and p38 MAPK, which are essential steps in the Duox-dependent production of reactive oxygen species (ROS) in response to intestinal bacterial infection (PubMed:25639794). During photoreceptor differentiation, it up-regulates transcription of Ubr3, which in turn promotes the hh- signaling pathway by mediating the ubiquitination and degradation of cos (PubMed:27195754, PubMed:25639794, PubMed:8166882, PubMed:1394430, PubMed:1340474, PubMed:11319862). FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (PubMed:7885476). In addition, the C-terminal part displays a cholesterol transferase activity that results by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Once cleaved, the C-product has no signaling activity and diffuses from the cell (PubMed:12586063). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm (PubMed:1280560). Also secreted in either cleaved or uncleaved form to mediate signaling to other cells (PubMed:1280560). SUBCELLULAR LOCATION: [Protein hedgehog N-product]: Cell membrane; Lipid-anchor Note=The N-terminal peptide remains associated with the cell surface (PubMed:12586063). Heparan sulfate proteoglycans of the extracellular matrix play an essential role in diffusion. Lipophorin is required for diffusion, probably by acting as vehicle for its movement, explaining how it can spread over long distances despite its lipidation (PubMed:15875013). SIMILARITY: Belongs to the hedgehog family.


FUNCTION: Synthesizes selenophosphate from selenide and ATP. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein Nucleus membrane; Peripheral membrane protein. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class II subfamily.


SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein.


FUNCTION: Mediates zinc uptake. May also transport other divalent cations. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. ZupT subfamily.


FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5- hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of feruloylated polysaccharides. Involved in the reinforcement of the plant cell wall. Also involved in the responding to wounding or pathogen challenge by the increased formation of cell wall-bound ferulic acid polymers. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily.


FUNCTION: Probable sesquiterpene synthase. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Lectin that functions as pattern recognizing receptor (PRR) specific for beta-1,3-linked and beta-1,6-linked glucans, which constitute cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and activation of NF-kappa-B: upon beta-glucan binding, recruits SYK via its ITAM motif and promotes a signaling cascade that activates some CARD domain-BCL10- MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation. Induces phosphorylation of SCIMP after binding beta-glucans. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.


FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.


FUNCTION: Myoactive; induces a rapid concentration-dependent muscle tension increase. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.


FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFB4 family.


FUNCTION: Chaperone protein that plays an important role in HCMV tropism. Cooperates with UL116 to regulate the abundance of gH-gL complexes in virion. Favors the incorporation of gL into virions once UL116 has regulated the early folding steps of virion assembly. Interacts with the host ERAD machinery and slows gO decay which would otherwise be constitutively degraded. Reorganizes the host endoplasmic reticulum and activates the unfolded protein response. Additionally, plays a role in the evasion of antiviral immune response by down- regulating cell surface expression of host CD58. Mechanistically, interacts with host CD58 and retains its immature form intracellularly. The capacity to cause endoplasmic reticulum reorganization and the intracellular retention of host CD58 are functionally independent properties. SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane; Single-pass type I membrane protein.


FUNCTION: May have cytolytic and antimicrobial activity. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL6 family.


FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (PubMed:3015618) (Probable). Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c family.


SIMILARITY: Belongs to the UPF0107 family.


FUNCTION: Structural subunit of the major fimbriae (PubMed:27062925). These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity. SUBCELLULAR LOCATION: Fimbrium Cell outer membrane Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein. SIMILARITY: Belongs to the bacteroidetes fimbrillin superfamily. FimA/Mfa1 family.


FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1 subfamily.


FUNCTION: Probably involved in the RNA silencing pathway and required for the generation of small interfering RNAs (siRNAs). SIMILARITY: Belongs to the RdRP family.


FUNCTION: Calcium-dependent prothrombin activator. This protein may activate prothrombin via recognition by the regulatory subunit of the calcium ion bound conformation of its gamma-carboxyglutamic acid (GLA) domain, and the subsequent conversion of prothrombin to active thrombin is catalyzed by the catalytic subunit. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family.


FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 654 nanometers (By similarity). SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family.


FUNCTION: Probable protein acetyltransferase with dual specificity triggering both N-alpha-acetylation (NTA) and epsilon-lysine acetylation (KA). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the acetyltransferase family. GNAT subfamily.


FUNCTION: Plays a role in carbon catabolite repression (CCR). Specifically required for transcriptional repression of the levanase operon by glucose but not by other sugars.


FUNCTION: In association with the non-catalytic regulatory subunit DHSp, catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF5A precursor protein to form the intermediate deoxyhypusine residue. Regulates protein levels of its regulatory subunit DHSp. Required for cell growth and survival. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the deoxyhypusine synthase family.


FUNCTION: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Associates with chromatin. SIMILARITY: Belongs to the MCMBP family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the MIT-like AcTx family.


FUNCTION: Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIId sub-subfamily.


FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the small Tim family.


FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane Cytoplasm, cytoskeleton, phragmoplast Secreted, cell wall Secreted, extracellular exosome Note=During cytokinesis, localizes to the nascent cell plate and later to the cell plate insertion site and along the post-cytokinetic wall (PubMed:20870962). Shuttles from the cytoplasm to the exocyst-positive organelle (EXPO) in the presence of EXO70E2 (PubMed:24307681). SIMILARITY: Belongs to the SEC6 family.


FUNCTION: Facilitates L-arginine uptake, as part of the AaxABC system. The arginine uptake by the bacterium in the macrophage may be a virulence factor against the host innate immune response (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OprB family.


SIMILARITY: Belongs to the arylamine N-acetyltransferase family.


FUNCTION: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'- nitrosonornicotine (NNN) (PubMed:19002761). Reductase that may be involved in a late step of tobacco alkaloid biosynthesis (PubMed:19002761). Maybe involved in either the formation of a nicotinic acid-derived precursor or the final condensation reaction of tobacco alkaloids (PubMed:19002761). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily.


FUNCTION: Oxidase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds (PubMed:24106156, PubMed:26414728). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP (PubMed:24106156). The enoyl reducrase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine (PubMed:24106156, PubMed:26414728). Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J (PubMed:26414728). The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation (PubMed:26414728). The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro- gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H (PubMed:26414728). Pyranonigrin H is substrate of pynH for dehydration- mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G (PubMed:26414728). The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E (PubMed:26414728). SIMILARITY: Belongs to the avfA family.


FUNCTION: PDI acts by binding stoichiometrically to cyclic nucleotide phosphodiesterase, changing the KM of the enzyme for cAMP from 10 uM to 2 mM.


FUNCTION: Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:29332244). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (PubMed:29332244). Involved in cell migration (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the ELP5 family.


FUNCTION: Transcriptional repressor involved in multiple aspects of cortical development, including neuronal migration, laminar and areal identity, and axonal projection (PubMed:9883721, PubMed:11239428, PubMed:21285371). As transcriptional repressor of FEZF2, it blocks the formation of the corticospinal (CS) tract from layer 6 projection neurons, thereby restricting the origin of CS axons specifically to layer 5 neurons (PubMed:21285371). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Bifunctional phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing two reactions of the de novo purine biosynthetic pathway. SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase family. Class II subfamily. SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase family.


FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


FUNCTION: Required for alpha-carboxysome (Cb) assembly, mediates interaction between RuBisCO and the Cb shell. The protein is probably intrinsically disordered. The C-terminal repeats act as the encapsulation signal to target proteins to the Cb; they are necessary and sufficient to target both CsoS2 and foreign proteins to the Cb. The N-terminal repeats of this protein bind simultaneously to both subunits of RuBisCO. Probably also interacts with the major shell proteins (CsoS1); that interaction would increase the local concentration of CsoS2 so that it can condense RuBisCO and full carboxysomes can be formed. SUBCELLULAR LOCATION: Carboxysome Note=This bacterium makes alpha-type carboxysomes. SIMILARITY: Belongs to the CsoS2 family.


FUNCTION: Cell surface receptor that binds to human complement C2a protein. This results in inhibition of the classical and lectin pathways of complement activation, probably due to interference with binding of C2a to C4b and interference with cleavage by C1 or MASP2 such that C3 convertase cannot be formed. This infers resistance to complement-mediated cell lysis, allowing parasite survival and infection (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Located on the surface tegumental plasma membrane, and tegumental surface pits of adult schistosomes so in contact with host blood plasma.


FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (By similarity). Contributes significantly to heme formation during erythropoiesis (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein Note=Localizes to the matrix side of the mitochondrion inner membrane. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.