FUNCTION: Monoglutamylase which modifies tubulin, adding a single glutamate on the gamma-carboxyl group of specific glutamate residues of target proteins (PubMed:32747782). Involved in the side-chain initiation step of the polyglutamylation reaction but not in the elongation step. Preferentially modifies beta-tail tubulin over the alpha-tubulin (PubMed:32747782). Involved in side-chain glutamylation of tubulin in sensory cilia (PubMed:20519502, PubMed:27635036, PubMed:29849065). Together with ttll-5 and ttll-11, required for male mating (PubMed:27635036). SIMILARITY: Belongs to the tubulin--tyrosine ligase family.


FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis- acting element (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group III family.


SIMILARITY: Belongs to the peptidase A31 family.


FUNCTION: Acts as a positive cofactor of GATA transcription factors to establish the identity of the ventral mesoderm during gastrulation. Down-regulation in the dorsal mesoderm is necessary for the proper formation of this territory since, when present, lmo4 may bind ldb1 and restrict the availability of this cofactor for Spemman organizer transcription factors. At neurula stages, suppresses primary neuron differentiation and modulates gene expression at the Isthmic Organizer of the midbrain-hindbrain boundary (By similarity).


FUNCTION: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the allene oxide cyclase family.


SIMILARITY: Belongs to the spermidine/spermine synthase family.


FUNCTION: Catalyzes the irreversible reduction of 2,3-butanediol to (S)-acetoin in the presence of NADH. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Repressor which binds to the hutP region in the histidine utilization (hut) operon. It blocks the expression of all the hut genes in the absence of inducer.


FUNCTION: Involved in the latter stages of lignin biosynthesis (PubMed:24985707). Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes (PubMed:25217505, PubMed:24985707). Mediates the conversion of feruloyl CoA to coniferylaldehyde (PubMed:25217505, PubMed:24985707). Also active toward p-coumaroyl-CoA and sinapoyl-CoA (PubMed:25217505, PubMed:24985707). Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (PubMed:24985707). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.


FUNCTION: Acts as a primer for viral genomic replication. DNA terminal protein is covalently linked to the 5'-ends of both strands of the genome through a phosphodiester bond between the beta-hydroxyl group of a tyrosine residue and the 5'-phosphate of the terminal deoxyadenylate. This protein is essential for DNA replication and is involved in the priming of DNA elongation (By similarity). SUBCELLULAR LOCATION: Virion. Host nucleus. SIMILARITY: Belongs to the tectivirus DNA terminal protein family.


SIMILARITY: Belongs to the UPF0107 family.


SIMILARITY: Belongs to the asfivirus B175L family.


FUNCTION: A structure-specific endonuclease that binds and cleaves the four-way Holliday junctions in DNA created during repair and rearrangement by the ubiquitous process of homologous recombination. Introduces paired nicks in opposing strands; on immobile junction cleaves 2 bases 3' of the junction point, on mobile strands the cleavage site varies. Cleaves Y and loop-out structures with much lower efficiency. Binds 4-way junction DNA but not sequence-identical linear dsDNA. SIMILARITY: Belongs to the Holliday junction resolvase Hjc family. Hje subfamily.


FUNCTION: Transcription factor that binds to DNA at the consensus sequence 5'-ACCAAAG-3' (PubMed:18505825, PubMed:18403418, PubMed:30190287). Acts as a transcriptional activator (PubMed:18505825, PubMed:18403418, PubMed:30190287). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (PubMed:18505825, PubMed:18403418). Involved in the differentiation of naive CD4-positive T-cells into peripherally induced regulatory T (pT reg) cells under inflammatory conditions (PubMed:30190287). Binds to the promoter region of the FOXP3 gene and promotes its transcription, and might thereby contribute to pT reg cell differentiation in the spleen and lymph nodes during inflammation (PubMed:30190287). Plays a redundant role with SOX4 and SOX11 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (PubMed:20596238). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: A cholesterol-dependent toxin that causes cytolysis by forming pores in cholesterol containing host membranes. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and formation of an oligomeric pore complex. Cholesterol is required for binding to host membranes, membrane insertion and pore formation; cholesterol binding is mediated by a Thr-Leu pair in the C-terminus. Acts as major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. Can be reversibly inactivated by oxidation. SUBCELLULAR LOCATION: Secreted Host membrane; Multi-pass membrane protein Host cell membrane; Multi-pass membrane protein Note=Secreted as soluble protein that then inserts into the host membrane and forms pores formed by transmembrane beta-strands. SIMILARITY: Belongs to the cholesterol-dependent cytolysin family.


FUNCTION: Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family.


FUNCTION: Motor protein that converts auditory stimuli to length changes in outer hair cells and mediates sound amplification in the mammalian hearing organ. Prestin is a bidirectional voltage-to-force converter, it can operate at microsecond rates. It uses cytoplasmic anions as extrinsic voltage sensors, probably chloride and bicarbonate. After binding to a site with millimolar affinity, these anions are translocated across the membrane in response to changes in the transmembrane voltage. They move towards the extracellular surface following hyperpolarization, and towards the cytoplasmic side in response to depolarization. As a consequence, this translocation triggers conformational changes in the protein that ultimately alter its surface area in the plane of the plasma membrane. The area decreases when the anion is near the cytoplasmic face of the membrane (short state), and increases when the ion has crossed the membrane to the outer surface (long state). So, it acts as an incomplete transporter. It swings anions across the membrane, but does not allow these anions to dissociate and escape to the extracellular space. Salicylate, an inhibitor of outer hair cell motility, acts as competitive antagonist at the prestin anion-binding site (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Lateral wall of outer hair cells. SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53) family.


FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (PubMed:14697203). Protein transport (By similarity). Probably involved in vesicular traffic (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (PubMed:14697203). FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (By similarity). Protein transport. Probably involved in vesicular traffic (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization. SIMILARITY: Belongs to the HPS/KGPDC family. KGPDC subfamily.


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


SIMILARITY: Belongs to the ViaA family.


FUNCTION: Component of the SWR1 complex which mediates the ATP- dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the actin family. ARP6 subfamily.


FUNCTION: Nucleotide-sugar transporter that transports UDP-rhamnose or UDP-galactose and UMP in a strict counter-exchange mode. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TPT transporter family. TPT (TC 2.A.7.9) subfamily.


FUNCTION: Bifunctional enzyme that catalyzes the formation of 4- diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D- erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4- diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C- methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF). SIMILARITY: In the C-terminal section; belongs to the IspF family. SIMILARITY: In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.


FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6- sialyltransferase activity toward oligosaccharides that have the Gal- beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family.


FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side.


FUNCTION: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Molybdate importer (TC 3.A.1.8) family.


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


SIMILARITY: Belongs to the Ntn-hydrolase family.


FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5- dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates phospholipase C and a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions from intracellular stores. Affects neural activity, perception, cognition and mood. Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, dendrite Cell projection, axon Cytoplasmic vesicle Membrane, caveola Presynapse. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: G-protein coupled receptor (PubMed:27072655). Has been shown to bind the neuroprotective and glioprotective factor prosaposin (PSAP), leading to endocytosis followed by an ERK phosphorylation cascade (PubMed:23690594). However, other studies have shown that prosaposin does not increase activity (PubMed:27072655, PubMed:28688853). It has been suggested that GPR37L1 is a constitutively active receptor which signals through the guanine nucleotide-binding protein G(s) subunit alpha (PubMed:27072655). Participates in the regulation of postnatal cerebellar development by modulating the Shh pathway (By similarity). Regulates baseline blood pressure in females and protects against cardiovascular stress in males (By similarity). Mediates inhibition of astrocyte glutamate transporters and reduction in neuronal N-methyl-D-aspartate receptor activity (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, cilium membrane; Multi-pass membrane protein Note=Associates with the basal membrane of Bergmann glia cell primary cilia. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield ADP. FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). SIMILARITY: In the N-terminal section; belongs to the NadD family. SIMILARITY: In the C-terminal section; belongs to the Ap4A hydrolase YqeK family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.


FUNCTION: Blocks voltage-gated potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 06 subfamily.


FUNCTION: Plays an important role in the elongation step of protein synthesis. SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.


FUNCTION: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.


FUNCTION: This toxin is described as enhancing presynaptic acetylcholine release, but neither experimental results, nor references to other sources are available. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Ancestral subfamily. Orphan group XIX sub-subfamily.


FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities. SUBCELLULAR LOCATION: Lysosome Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule. SIMILARITY: Belongs to the pancreatic ribonuclease family.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily.


FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this organism) is implicated in DNA promoter recognition and in nucleotide binding. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA polymerase beta chain family.


FUNCTION: Efficient protease with alanine specificity but only little elastolytic activity. SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.


FUNCTION: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP. FUNCTION: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AgrB family. SIMILARITY: Belongs to the AgrB family.


FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm. SUBCELLULAR LOCATION: Virion Virion tegument Host cytoplasm Host Golgi apparatus. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 1 family.


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


FUNCTION: Involved in cell shape control. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CetZ family.


FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2- cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). SUBCELLULAR LOCATION: Cytoplasm Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Note=May associate with the mitochondrion outer membrane. SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. QTRT2 subfamily.


FUNCTION: May function as an ionophore.


SIMILARITY: Belongs to the UPF0181 family.


SUBCELLULAR LOCATION: Host cytoplasm Host mitochondrion Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus A NSP6 family.


FUNCTION: Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. SUBCELLULAR LOCATION: Nucleus Note=Found in the oocyte nucleus before nuclear membrane breakdown, after which it is redistributed to the cytoplasm. SIMILARITY: Belongs to the nucleoplasmin family.


FUNCTION: Mediates the efflux of short-chain diamines when energized by an electrochemical gradient (By similarity). Confers resistance to chlorhexidine, benzalkonium, proflavine and acriflavine. Mediates efflux of both proflavine and acriflavine via an energy-dependent mechanism (PubMed:25670776). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the proteobacterial antimicrobial compound efflux (PACE) (TC 2.A.117) family.


SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsaM family.


FUNCTION: Binds to tRNA and functions as a cofactor for the methionyl- tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C- terminal part (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the tRNA-aminoacylation cofactor ARC1 family.


FUNCTION: Possesses a potent antimicrobial activity against Gram- positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.


FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. FUNCTION: Forms part of the polypeptide exit tunnel. FUNCTION: Forms part of the polypeptide exit tunnel. FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). FUNCTION: This protein when expressed in E.coli represses both transcription and translation of the endogenous S10 operon. As the H.influenzae S10 leader can be regulated in vitro by the E.coli L4 protein this strongly suggests the endogenous protein controls its own S10 operon in a similar fashion. FUNCTION: Protein L4 is a both a transcriptional repressor and a translational repressor protein. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader. L4 controls the translation of the S10 operon by binding to its mRNA (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uL4 family. SIMILARITY: Belongs to the universal ribosomal protein uL4 family.


FUNCTION: Bifunctional serine/threonine kinase and phosphorylase involved in the dark/light-mediated regulation of PPDK by catalyzing its phosphorylation/dephosphorylation. Has a much lower phosphotransferase activity than PDRP1 (PubMed:21883547). Can use ADP as a high specificity substrate and GDP as a lower affinity substrate, but has no activity with UDP (PubMed:21414960). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase regulatory protein family. PDRP subfamily.


FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II- dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF12 family.


FUNCTION: Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G- protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C and adenylyl cyclase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Enhances the translation of downstream ORFs on polycistronic mRNAs derived from carnation etched ring virus. SUBCELLULAR LOCATION: Host cytoplasm. Note=Found in cytoplasmic occlusion bodies. SIMILARITY: Belongs to the caulimoviridae viroplasmin family.


FUNCTION: This protein binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family.


FUNCTION: May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins. SUBCELLULAR LOCATION: Photoreceptor inner segment Cell projection, cilium, photoreceptor outer segment. SIMILARITY: Belongs to the arrestin family.


FUNCTION: Could be implicated in the processing or the export process of the lantibiotic lacticin 481/lactococcin DR.


FUNCTION: Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the U1 small nuclear ribonucleoprotein C family.


FUNCTION: Ca(2+)-independent actin-binding protein. Binds actin microfilaments (MFs). Involved in actin filament bundling, severing and capping. Caps the barbed end of actin filaments and protects them from disassembly. Promotes VLN3-mediated MF severing. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the villin/gelsolin family.


FUNCTION: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine and the release of L-ornithine from [LysW]-L-ornithine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M20A family. LysK subfamily.


FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp). Can also methylate cytosine 38 in tRNA(Glu), albeit to a lower level, but not tRNA(Lys). Pmt1-dependent tRNA methylation is induced by nitrogen limitation and depends on the nutrient-sensing protein kinase sck2. Does not have DNA-methylation activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the snail C2H2-type zinc-finger protein family.


FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.


SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.


FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3- containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Chromosome, centromere, kinetochore Note=Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore, and may connect it to the outer kinetochore via its N-terminus. SIMILARITY: Belongs to the CENP-T/CNN1 family.


FUNCTION: Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that shows proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN. Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration. Participates in the development of brown adipose tissue and browning of white adipose tissue. Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.


FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. PQQ is probably formed by cross-linking a specific glutamate to a specific tyrosine residue and excising these residues from the peptide (By similarity). FUNCTION: Required for coenzyme pyrroloquinoline quinone (PQQ) biosynthesis. PQQ is probably formed by cross-linking a specific glutamate to a specific tyrosine residue and excising these residues from the peptide. SIMILARITY: Belongs to the PqqA family. SIMILARITY: Belongs to the PqqA family.


FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(i)-alpha and G(o)-alpha, but not to G(s)-alpha (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm Membrane. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.


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


FUNCTION: Tyrosine kinase involved in the regulation of tissues remodeling (PubMed:30449416). It functions as cell surface receptor for fibrillar collagen and regulates cell differentiation, remodeling of the extracellular matrix, cell migration and cell proliferation. Required for normal bone development. Regulates osteoblast differentiation and chondrocyte maturation via a signaling pathway that involves MAP kinases and leads to the activation of the transcription factor RUNX2. Regulates remodeling of the extracellular matrix by up- regulation of the collagenases MMP1, MMP2 and MMP13, and thereby facilitates cell migration and tumor cell invasion. Promotes fibroblast migration and proliferation, and thereby contributes to cutaneous wound healing. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I20 (potato type II proteinase inhibitor) family.


FUNCTION: Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the HIN-200 family.


FUNCTION: Involved in the non-oxidative decarboxylation and detoxification of phenolic derivatives under both aerobic and anaerobic conditions (PubMed:18388975). Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for phenolic acid decarboxylase (By similarity). SIMILARITY: Belongs to the UbiX/PAD1 family. YclB subfamily.


FUNCTION: Possesses antiviral potency. Inhibits viral infection of plants (tobacco mosaic virus) (PubMed:10403789). Inhibits protein synthesis in both prokaryotes and eukaryotes (PubMed:8034016, PubMed:10403789). SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.


FUNCTION: Gamma-glutamyl cyclotransferase-like protein; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L- tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L- serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT- mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Transcription factor required for the development of the heart and the spleen (PubMed:9584153, PubMed:19483677, PubMed:22560297). During heart development, acts as a transcriptional activator of NPPA/ANF in cooperation with GATA4 (PubMed:9584153). May cooperate with TBX2 to negatively modulate expression of NPPA/ANF in the atrioventricular canal (PubMed:12023302). Binds to the core DNA motif of NPPA promoter (PubMed:19483677). Together with PBX1, required for spleen development through a mechanism that involves CDKN2B repression (PubMed:22560297). Positively regulates transcription of genes such as COL3A1 and MMP2, resulting in increased pulmonary endothelial fibrosis in response to hypoxia (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NK-2 homeobox family.


FUNCTION: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. FUNCTION: Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at mid-cell. SUBCELLULAR LOCATION: Cytoplasm Note=Localizes at mid-cell. SIMILARITY: Belongs to the ZapA family. Type 1 subfamily. SIMILARITY: Belongs to the ZapA family. Type 1 subfamily.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family.


FUNCTION: Plays an essential role in budded virion (BV) and occluded derived virion (ODV) development. Participates in intranuclear microvesicle formation, ODV envelopment, and subsequent embedding of virions into occlusion bodies. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus.


FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds (PubMed:24106156). 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 paxM FAD-dependent monooxygenase family.


FUNCTION: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Phi family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 08 (U8-Lctx) subfamily.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFB8 subunit family.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). Required for proper protein synthesis within the mitochondrion. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the GatF family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0324 family.


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


FUNCTION: Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion (PubMed:17226786, PubMed:20819079). May potentiate mitogenesis induced by the neuropeptide bombesin by mediating an increase in the duration of MAPK1/3 (ERK1/2) signaling, which leads to accumulation of immediate-early gene products including FOS that stimulate cell cycle progression (PubMed:17226786). In response to oxidative stress, is phosphorylated at Tyr-438 and Tyr-718 by ABL1, which leads to the activation of PRKD2 without increasing its catalytic activity, and mediates activation of NF-kappa-B (By similarity). In response to the activation of the gastrin receptor CCKBR, is phosphorylated at Ser-244 by CSNK1D and CSNK1E, translocates to the nucleus, phosphorylates HDAC7, leading to nuclear export of HDAC7 and inhibition of HDAC7 transcriptional repression of NR4A1/NUR77 (By similarity). Upon TCR stimulation, is activated independently of ZAP70, translocates from the cytoplasm to the nucleus and is required for interleukin-2 (IL2) promoter up-regulation. During adaptive immune responses, is required in peripheral T-lymphocytes for the production of the effector cytokines IL2 and IFNG after TCR engagement and for optimal induction of antibody responses to antigens (PubMed:20819079). In epithelial cells stimulated with lysophosphatidic acid (LPA), is activated through a PKC-dependent pathway and mediates LPA-stimulated interleukin-8 (IL8) secretion via a NF-kappa-B-dependent pathway (By similarity). During TCR-induced T-cell activation, interacts with and is activated by the tyrosine kinase LCK, which results in the activation of the NFAT transcription factors (By similarity). In the trans-Golgi network (TGN), regulates the fission of transport vesicles that are on their way to the plasma membrane and in polarized cells is involved in the transport of proteins from the TGN to the basolateral membrane (By similarity). Plays an important role in endothelial cell proliferation and migration prior to angiogenesis, partly through modulation of the expression of KDR/VEGFR2 and FGFR1, two key growth factor receptors involved in angiogenesis (By similarity). In secretory pathway, is required for the release of chromogranin-A (CHGA)-containing secretory granules from the TGN (By similarity). Downstream of PRKCA, plays important roles in angiotensin-2-induced monocyte adhesion to endothelial cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Golgi apparatus, trans-Golgi network Note=Translocation to the cell membrane is required for kinase activation. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled receptors. Nuclear accumulation is regulated by blocking nuclear export of active PRKD2 rather than by increasing import. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. PKD subfamily.


FUNCTION: Binds actin monomers (G actin) and plays a role in the reorganization of the actin cytoskeleton and in formation of actin stress fibers. SUBCELLULAR LOCATION: Cytoplasm Synapse Nucleus Note=Enriched at synapses (By similarity). Cytoplasmic in resting cells, and is imported into the nucleus upon serum stimulation. Interaction with actin prevents nuclear import (By similarity). SIMILARITY: Belongs to the phosphatase and actin regulator family.


FUNCTION: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1- aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Forms part of the polypeptide exit tunnel. FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity). FUNCTION: This protein when expressed in E.coli represses both transcription and translation of the endogenous S10 operon. As the M.morganii S10 leader can be regulated in vitro by the E.coli L4 protein this strongly suggests the endogenous protein controls its own S10 operon in a similar fashion. FUNCTION: Protein L4 is a both a transcriptional repressor and a translational repressor protein. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader. L4 controls the translation of the S10 operon by binding to its mRNA (By similarity). SIMILARITY: Belongs to the universal ribosomal protein uL4 family.


FUNCTION: The GINS complex plays an essential role in the initiation of DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the GINS3/PSF3 family.


FUNCTION: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor. Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons. Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16. SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor Cytoplasmic vesicle membrane; Lipid-anchor Cytoplasm Cell projection, axon Note=Delivered to axons with Golgi- derived cytoplasmic vesicles. SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.


FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. SIMILARITY: Belongs to the glucose-1-phosphate thymidylyltransferase family.


FUNCTION: Transcriptional repressor of genes that require a bHLH protein for their transcription. SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: To A.fulgidus AF_1225.


FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NhaB Na(+)/H(+) (TC 2.A.34) antiporter family.


FUNCTION: Probable membrane-remodeling GTPase that plays a unique role in the in the determination of thylakoid and chloroplast morphology and regulates organization of the thylakoid network. Not involved in the determination of mitochondrial morphology or ultrastructure. SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Multi-pass membrane protein Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein Note=Localizes in a punctate pattern in chloroplasts. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.


FUNCTION: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including PACC itself) and represses transcription of acid- expressed genes. Specifically recognizes and binds the consensus sequence 5'-GCCARG-3'. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the pacC/RIM101 family.


FUNCTION: Required for the maintenance of the structure of the mitochondrial inner membrane. Involved in mitochondrial morphology. Causes growth arrest when highly overexpressed (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SHE9 family.


FUNCTION: Shell component of a type 2A encapsulin nanocompartment. Forms encapsulin nanocompartments about 24 nm in diameter from 60 monomers, probably involved in sulfur metabolism (By similarity). Probably encapsulates cysteine desulfurase (Probable). SUBCELLULAR LOCATION: Encapsulin nanocompartment Cell membrane. SIMILARITY: Belongs to the encapsulin family. Family 2A subfamily.


FUNCTION: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors. SUBCELLULAR LOCATION: Virion tegument. Host nucleus Note=Localizes to the centrosome and more precisely to the periphery of the centriole, tightly encircling the tubulin-rich centrioles. SIMILARITY: Belongs to the herpesviridae thymidine kinase family.


SIMILARITY: Belongs to the Smg family.


FUNCTION: Major constituent of messenger ribonucleoprotein particles (mRNPs) (PubMed:10076007, PubMed:12297523, PubMed:12648488). Involved in the regulation of the stability and/or translation of germ cell mRNAs (PubMed:15031116). Binds to Y-box consensus promoter element (PubMed:10076007, PubMed:12297523, PubMed:12648488). Binds to full- length mRNA with high affinity in a sequence-independent manner (PubMed:10076007, PubMed:12297523, PubMed:12648488). Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity (PubMed:10076007, PubMed:12297523, PubMed:12648488). Its binding with maternal mRNAs is necessary for its cytoplasmic retention (PubMed:10076007, PubMed:12297523, PubMed:12648488). May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (PubMed:15665108). SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Hemextin AB complex: specifically inhibits the activation of FX (F10) by the TF-FVIIa complex (extrinsic tenase complex (ETC)) (IC(50)= 100 nM, Ki=25 nM) by non-competitively inhibiting the enzymatic activity of FVIIa. FUNCTION: Hemextin A (monomer): exhibits mild anticoagulant activity. It specifically inhibits the activation of FX (F10) by the TF-FVIIa complex (extrinsic tenase complex (ETC)) by non-competitively inhibiting the enzymatic activity of FVIIa. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type IB cytotoxin sub-subfamily.


FUNCTION: Could be involved in calcium metabolism in pollen. Binds 3 calcium ions.


FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. Inhibits the activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38 by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively regulates leukotriene production in neutrophils (By similarity). Negative regulator of hematopoietic progenitor cell proliferation, survival and migration. Critical regulator of thymocyte development and T-cell antigen receptor (TCR) signaling by mediating recruitment and activation of ZAP70 (PubMed:17028588). Required for phosphorylation of CD3Z, membrane translocation of ZAP70 and subsequent activation of the ZAP70-mediated pathways. Essential for efficient beta-selection and positive selection by promoting the ZAP70-dependent phosphorylation of the LAT signalosome during pre-TCR and TCR signaling. Crucial for thymocyte maturation during DN3 to DN4 transition and during positive selection. Plays critical roles in mast cell function by facilitating phosphorylation of SYK in Fc epsilon RI-mediated signal transduction. Essential for the phosphorylation of LAT, LCP2, PLCG1 and PLCG2 and for Ca(2+) mobilization in mast cells. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Lipid-anchor; Cytoplasmic side Note=Colocalizes together with ZAP70 in the immunological synapse. SIMILARITY: Belongs to the small GTPase superfamily. Rho family.


FUNCTION: Stimulates the DNA unwinding activity of PriA helicase, which does not seem to require single-stranded DNA-binding by PriB. Activates DNA-dependent ATP hydrolysis catalyzed by PriA. SIMILARITY: Belongs to the PriB family.


FUNCTION: Serine/threonine protein kinase involved in regulation of exocytosis. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. NIM1 subfamily.


SIMILARITY: Belongs to the TMA7 family.


FUNCTION: Major seed storage protein. SUBCELLULAR LOCATION: Vacuole, aleurone grain. Vacuole. Note=Cotyledonary membrane-bound vacuolar protein bodies. SIMILARITY: Belongs to the 7S seed storage protein family.


FUNCTION: Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly. Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature. In addition to binding to clathrin, mediates the endocytosis of small R- SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8. In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors. Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF). SUBCELLULAR LOCATION: Cell membrane Membrane, clathrin-coated pit Golgi apparatus Cytoplasmic vesicle, clathrin-coated vesicle Nucleus Note=Colocalized with clathrin in the Golgi area. Interaction with PIMREG may target PICALM to the nucleus in some cells. SIMILARITY: Belongs to the PICALM/SNAP91 family.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A- phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PTPA-type PPIase family.


FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Rho-1 GABA receptor could play a role in retinal neurotransmission (By similarity). SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi- pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRR1 sub- subfamily.


FUNCTION: Acts as a receptor for the Gram-negative bacterium F.nucleatum. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Putative tyrosine recombinase. Not involved in the cutting and rejoining of the recombining DNA molecules on dif(SL) site. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerD-like subfamily.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL41 family.


FUNCTION: Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the FlgA family.


FUNCTION: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Note=Outer membrane- anchored. SIMILARITY: Belongs to the Tom5 family.


FUNCTION: Acts as a backup for CMTM6 to regulate plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity. May protect PD- L1/CD274 from being polyubiquitinated and targeted for degradation. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the chemokine-like factor family.


FUNCTION: Probably targets cAMP-dependent protein kinase (PKA) to the cellular membrane or cytoskeletal structures. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium (By similarity). Isoform Delta may be involved in shuttling aquaporin-2 (AQP2) to the plasma membrane. SUBCELLULAR LOCATION: [Isoform Gamma]: Nucleus Cytoplasm. SUBCELLULAR LOCATION: [Isoform Delta]: Nucleus Cell membrane Note=Cotranslocates with AQP2 to the plasma membrane in response to arginine-vasopressin (AVP) stimulation in inner medullary collecting duct (IMCD) cells.


FUNCTION: Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo. Also acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.


FUNCTION: Scaffolding protein that specifically recognizes and binds dimethylarginine-containing proteins. Plays a role in the regulation of translation of target mRNAs by binding Arg/Gly-rich motifs (GAR) in dimethylarginine-containing proteins. In nucleus, acts as a coactivator: recognizes and binds asymmetric dimethylation on the core histone tails associated with transcriptional activation (H3R17me2a and H4R3me2a) and recruits proteins at these arginine-methylated loci. In cytoplasm, acts as an antiviral factor that participates in the assembly of stress granules together with G3BP1. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. Associated with actively translating polyribosomes. Component of stress granules.


FUNCTION: Putative transcription activator involved in regulating light control of development. SUBCELLULAR LOCATION: Nucleus Note=The nuclear localization is independent of the light treatment. SIMILARITY: Belongs to the FHY3/FAR1 family.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Associates with the inner membrane via RseA. SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.


FUNCTION: Amino acid transporter. 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.18.2) subfamily.


FUNCTION: Involved in the synthesis of Nod factor, a sulfated N-acyl- beta-1,4-tetrasaccharide of N-acetylglucosamine which initiates a series of events in the host plant species leading eventually to nodulation. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the NodC/HAS family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AAE transporter (TC 2.A.81) family. YidE subfamily.


FUNCTION: Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 13-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation. SUBCELLULAR LOCATION: Secreted Note=Synthesized by the mid and distal caput of the epididymis and secreted into the epididymal lumen. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: Essential protein that is involved in the control of cell division, probably through the regulation of ctrA. Its phosphorylation status is regulated by PdhS (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Localized at one pole of the cell. Colocalizes with PdhS (By similarity).


SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the strictosidine synthase family.


SIMILARITY: In the C-terminal section; belongs to the PhoH family.


FUNCTION: Acts as a component of the auxin efflux carrier. Seems to be involved in the polar auxin transport which may promote adventitious root emergence and control tillering. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69.1) family.


FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N- acetylglucosamine-6-phosphate (GlcNAc-6-P). SIMILARITY: Belongs to the NanE family.


FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Also acts as a disulfide oxidoreductase in cytochromes c biogenesis. The cysteines of apocytochromes c must be in the reduced state for covalent linkage between the two moieties to occur (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.


FUNCTION: Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the FKBP-type PPIase family.


FUNCTION: Catalyzes the NADH-dependent reduction of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5- methyltetrahydrofolate. FUNCTION: Catalyzes the NADH-dependent reduction of 5,10- methylenetetrahydrofolate to 5-methyltetrahydrofolate (PubMed:9922232). Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate. Can also use NADPH as the reductant, but much less effectively than NADH (PubMed:9922232). SIMILARITY: Belongs to the methylenetetrahydrofolate reductase family.


SIMILARITY: Belongs to the DapA family.


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


FUNCTION: Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites. FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:9872316, PubMed:9872744, PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10906333, PubMed:10773016, PubMed:10075644, PubMed:9872744, PubMed:24305054). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine- tuning of inhibitory synaptic transmission (PubMed:9844003). Pre- synaptic GABA receptor inhibits neurotransmitter release by down- regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:9844003, PubMed:9872316, PubMed:10075644, PubMed:9872744, PubMed:22660477). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). Activated by (-)-baclofen, cgp27492 and blocked by phaclofen (PubMed:9844003, PubMed:9872316, PubMed:24305054). SUBCELLULAR LOCATION: [Isoform 1E]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane; Multi-pass membrane protein Cell projection, dendrite Note=Colocalizes with ATF4 in hippocampal neuron dendritic membranes (By similarity). Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane (PubMed:15617512). SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily.


FUNCTION: Involved in pristinamycin I biosynthesis (PubMed:9044253). Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from chorismate and glutamine (By similarity). SIMILARITY: In the C-terminal section; belongs to the anthranilate synthase component I family.


FUNCTION: Acts as a weak IFN antagonist. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the phlebovirus NS-S protein family.


FUNCTION: E3 ubiquitin-protein ligase that plays a key role in endosome organization by retaining vesicles in the perinuclear cloud (PubMed:27368102). Acts as a platform for perinuclear positioning of the endosomal system by mediating ubiquitination of SQSTM1 through interaction with the ubiquitin conjugating enzyme UBE2J1 (PubMed:27368102, PubMed:33472082). Ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Also acts as a regulator of type I interferon production in response to viral infection by mediating the formation of 'Lys-11'-linked polyubiquitin chains on TMEM173/STING, leading to stabilize TMEM173/STING (PubMed:25254379, PubMed:32614325). Also required to limit type I interferon response by promoting autophagic degradation of IRF3 (PubMed:25254379). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: Nucleoside diphosphate sugar hydrolase that hydrolyzes GDP- mannose as its preferred substrate, yielding GMP and mannose-1- phosphate. SIMILARITY: Belongs to the Nudix hydrolase family. NudK subfamily.


FUNCTION: RNA-binding protein that plays an essential role in spermatogenesis. May act by binding to the 3'-UTR of mRNAs and regulating their translation. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. Nuclear at some stages of spermatozoide development. Localizes both to the nuclei and cytoplasm of spermatozoide differentiation. Nuclear in fetal gonocytes and in spermatogonial nuclei. It then relocates to the cytoplasm during male meiosis. SIMILARITY: Belongs to the RRM DAZ family.


FUNCTION: Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene). SIMILARITY: Belongs to the carotenoid oxygenase family.


FUNCTION: Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antagonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter (By similarity). FUNCTION: Acts as a transcriptional regulator in bone development. Represses the ALPL promoter activity and antagonizes the stimulatory effect of DLX5 on ALPL expression during osteoblast differentiation. Probable morphogenetic role. May play a role in limb-pattern formation. In osteoblasts, suppresses transcription driven by the osteocalcin FGF response element (OCFRE). Binds to the homeodomain-response element of the ALPL promoter. SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Msh homeobox family.


FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination of various substrates (PubMed:23645206, PubMed:25165885). In turn, participates in the regulation of many biological processes including cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive immunity (PubMed:25165885, PubMed:28708287). Acts as negative regulator of NF-kappa-B-dependent transcription by promoting the ubiquitination and stabilization of the NF-kappa-B inhibitor TNFAIP3 (PubMed:25165885). May promote the ubiquitination of TRAF6 as well (PubMed:28708287). Acts also as a negative regulator of T-cell activation (PubMed:25165885). Inhibits cellular dsRNA responses and interferon production by targeting MAVS component for proteasomal degradation (PubMed:25165885). Ubiquitinates the CDK inhibitor CDKN1A leading to its degradationand probably also CDKN1B and CDKN1C (PubMed:23645206). This activity stimulates cell cycle G1-to-S phase transition and suppresses cellular senescence. May play a role in spermatogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Essential for sporulation. Interferes with or is a negative regulator of the pathway leading to asymmetric septation. SIMILARITY: Belongs to the SpoVG family.


FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn- glycerol-3-phosphate (G3P) import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. sn-glycerol-3- phosphate importer (TC 3.A.1.1.3) family.


SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the WD repeat WDR3/UTP12 family.


FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the rad1 family.


FUNCTION: Proton-coupled monocarboxylate symporter (PubMed:21792931). Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in transporting substrate (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm Basolateral cell membrane; Multi-pass membrane protein Note=Requires the ancillary protein, EMB for plasma membrane localization (By similarity). Colocalizes with BSG in spermatozoa. Detected in the cytoplasm of Sertoli cells (PubMed:21792931). SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.


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


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


FUNCTION: Catalyzes the conversion of isovaleryl-CoA/3-methylbutanoyl- CoA to 3-methylbut-2-enoyl-CoA as an intermediate step in the leucine (Leu) catabolic pathway. To a lesser extent, is also able to catalyze the oxidation of other saturated short-chain acyl-CoA thioesters as pentanoyl-CoA, hexenoyl-CoA and butenoyl-CoA. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.


FUNCTION: Antibacterial peptide with activity against Gram-positive and Gram-negative bacteria (By similarity). May also be active against fungi (Probable). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL36 family.


SIMILARITY: Belongs to the FAM131 family.


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


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


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


SUBCELLULAR LOCATION: Lysosome.


FUNCTION: Is believed to be a multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing. At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades. Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93. In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK. Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading. Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway. Required for protein synthesis in mitochondria. In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA- binding activity. May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles. Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation. Is required for the nuclear translocation of splicing factor U2AF1L4. Involved in regulation of CDKN2A- and HRK-mediated apoptosis. May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription. May play a role in antibacterial defense. FUNCTION: (Microbial infection) During bacterial infection processes acts as an attachment site for microbial proteins, including Listeria monocytogenes internalin B (InlB). SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Cell membrane; Peripheral membrane protein; Extracellular side Secreted Cytoplasm Nucleus, nucleolus Note=Seems to be predominantly localized to mitochondria. Secreted by activated lymphocytes. SIMILARITY: Belongs to the MAM33 family.


FUNCTION: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Archaeal CCA-adding enzyme subfamily.


FUNCTION: Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the WRB/GET1 family.


FUNCTION: Positive modulator of ATM response to DNA damage. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytosol Nucleus Note=Cytoplasmic under growth arrest conditions. Translocated into the nucleus when growth resumes (S phase) and following DNA damage.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.


FUNCTION: Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt- dependent activation of FZD4, suggesting the existence of a Wnt- independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction. SUBCELLULAR LOCATION: Secreted.


FUNCTION: May act as receptor for class I MHC antigens. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the HMG-CoA reductase family.


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


FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Required for proper rRNA processing and maturation of 18S rRNAs. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family.


FUNCTION: Directs RNA polymerase II nuclear import. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the IWR1/SLC7A6OS family.


FUNCTION: This enzyme is an effector of chloramphenicol resistance in bacteria. SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase delta chain family.


SIMILARITY: Belongs to the ninE family.


SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein.


FUNCTION: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase T1A family.


FUNCTION: May have a role in early embryogenesis. SIMILARITY: Belongs to the gonadal family.


FUNCTION: May act as an apoptosis inhibitor.


FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2F/RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.


FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose (PubMed:23481255, PubMed:23474714, PubMed:21849506). Specifically acts as a glutamate mono-ADP- ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to glutamate residues on proteins (PubMed:23481255, PubMed:23474714). Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG to become a substrate for OARD1 (PubMed:23481255). Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins (PubMed:21849506). Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O- butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively (PubMed:21849506). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus, nucleolus Chromosome Note=Localizes both in the nucleoplasm and in the nucleolus (PubMed:29712969). Relocalizes to the nucleoplasm in response to DNA damage (PubMed:29712969). Recruited to DNA lesion regions following DNA damage (PubMed:23481255).


FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:11229364). Regulates the activation of NF- kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum Note=Not secreted. SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 05 (agouti) family.


FUNCTION: Catalyzes the conversion of threonine to 2-oxobutanoate and ammonia. Functions in the threonine-dependent pathway of isoleucine biosynthesis, which is the minor pathway for isoleucine biosynthesis in G.sulfurreducens. Also displays serine ammonia-lyase activity, yielding pyruvate from L-serine. SIMILARITY: Belongs to the serine/threonine dehydratase family.


FUNCTION: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4- dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the LanC-like protein family.


FUNCTION: Conversely, a more recent study suggests an alternative function of CydDC: authors suggest that CydDC does not mediate the export of L-cysteine but rather reduces cytoplasmic L-cystine to L- cysteine (PubMed:32900959). The principle function of CydDC would be to maintain the reduced state of cytoplasmic L-cysteine, thereby providing an important connection between sulfur metabolism, oxidative stress and resistance to antibiotics (PubMed:32900959). FUNCTION: Part of the ABC transporter complex CydDC that exports the reduced low-molecular-weight thiols cysteine and glutathione to the periplasm (PubMed:12393891, PubMed:16040611). Export of these thiol- containing redox-active molecules may be crucial for redox homeostasis in the periplasm, permitting correct assembly of various respiratory complexes and formation of correct disulfide bonds in periplasmic and secreted proteins (Probable). CydD contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation (PubMed:24958725). Required for the assembly of functional cytochrome bd-type quinol oxidases and periplasmic c-type cytochromes (PubMed:7934832, PubMed:8181727, PubMed:15470119). Overexpression of CydDC under anaerobic conditions also results in the formation of a heme biosynthesis-derived pigment, P-574 (PubMed:12375104). CydDC binds heme b, but heme is probably not transported by the complex and instead has a role in regulating ATPase activity (PubMed:24958725). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Cysteine exporter (TC 3.A.1.129.1) family.


FUNCTION: Involved in lignin biosynthesis (PubMed:16443696, PubMed:21912859). Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde and sinapaldehyde to their respective alcohols (PubMed:16443696). Plays the major role in monolignol biosynthesis. Functions cooperatively with COMT in the culm internodes for the biosynthesis of monolignols, the lignin precursors. May be involved in lignin biosynthesis in leaves and roots (PubMed:21912859). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins).


FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly to apatite and calcium. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.


FUNCTION: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation-acylation reaction to produce phosphatidylglycerol-36:1. May be involved in bis(monoacylglycerol)phosphate biosynthetic pathway (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Endoplasmic reticulum Mitochondrion Note=Localizes at the endoplasmic reticulum and at the endoplasmic reticulum-mitochondria interface. SIMILARITY: Belongs to the SERAC1 family.


FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-1 targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit M family.


FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


FUNCTION: Induces sprouting in endothelial cells through an autocrine and paracrine action. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Probable secreted metalloprotease that shows high activities on basic nuclear substrates such as histone and protamine (By similarity). May be involved in virulence. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M35 family.


FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. Plays a central role in positioning the mitotic spindle at the bud neck during cell division. Targets cytoplasmic dynein to microtubule plus ends, thereby promoting dynein- mediated microtubule sliding along the bud cortex and consequently the movement of the mitotic spindle to the bud neck. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules and the mitotic spindle poles. SIMILARITY: Belongs to the WD repeat LIS1/nudF family.


SIMILARITY: Belongs to the AKNA family.


FUNCTION: Glycosyltransferase involved in the xylosylation of N-glycans (PubMed:10781814, PubMed:12943552, PubMed:15013764, PubMed:15686448). Possesses beta-1,2-xylosyltransferase activity, transferring xylose from UDP-xylose to the core beta-linked mannose of N-glycans (PubMed:10781814, PubMed:12943552, PubMed:15013764, PubMed:15686448). Involved in the biosynthesis of glycoprotein bound N-glycans (PubMed:15686448, PubMed:22024534). Does not require metal ions for its activity (PubMed:15686448). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Note=Localizes in medial cisternae of Golgi apparatus.


FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the peptidase M17 family.