FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of acetylaranotin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide-bridged cyclic dipeptide (PubMed:23586797). The first step of acetylaranotin biosynthesis is performed by the NRPS ataP which produces diketopiperazine cyclo-L-Phe-L-Phe via the condensation of 2 phenylalanines (L-Phe) (PubMed:23586797). The ataC domain of ataTC then catalyzes the formation of bishydroxylation of cyclo-L-Phe-L-Phe (PubMed:23586797). The glutathione S-transferase domain ataG in ataIMG further catalyzes the conjugation of two glutathiones to the bishydroxylated intermediate (PubMed:23586797). Next, the dipeptidase ataJ removes the Glu residues (PubMed:23586797). The following step is performed by the carbon sulfur lyase domain ataI of ataIMG which may convert the bis-cysteinyl adduct to yield an epidithiol intermediate (PubMed:23586797). The ataT domain from ataTC then catalyzes the oxidation of the free dithiols, followed by a cyclization step catalyzed by the cytochrome P450 ataF (PubMed:23586797). AtaF probably acts as an epoxidase to promote a dual epoxidation formation at C8 and C9 along with C8' and C9', followed by the spontaneous nucleophilic attack of the amide nitrogens N10 and N10' to yield an intermediate with the pyrrolidine partial structure (PubMed:23586797). The final steps of acetylaranotin biosynthesis involve the acetylation and ring rearrangement of an epitetrathiodiketopiperazine intermediate to produce acetylaranotin (PubMed:23586797). AtaH probably catalyzes the acetylation of epitetrathiodiketopiperazine to produce a diacetate and ataY is responsible for the formation of the dihydrooxepin moiety that converts the diacetate intermediate to acetylaranotin via acetylapoaranotin (PubMed:23586797). Both enzymes could function independently in the absence of the other (PubMed:23586797). The specific function of ataL within the pathway has still to be determined (PubMed:23586797). The acetylaranotin bis-thiomethyltransferase ataS located outside of acetylaranotin gene cluster is the main thiomethyltransferase responsible for converting acetylaranotin and its related intermediates to their methylated forms (PubMed:30096370).


FUNCTION: The A* protein binds to double-stranded DNA and prevents their hydrolysis by nucleases. FUNCTION: The A protein is a specific endonuclease that cleaves the viral strand of supertwisted, closed circular DNA at a unique site in the A gene. The A protein also causes relaxation of supertwisted DNA and forms a complex with viral DNA that has a discontinuity in gene A of the viral strand.


FUNCTION: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). SRP9 together with SRP14 and the Alu portion of the SRP RNA, constitutes the elongation arrest domain of SRP (By similarity). The complex of SRP9 and SRP14 is required for SRP RNA binding (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SRP14 family.


FUNCTION: Putative cyclic nucleotide-gated ion channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family.


FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.


FUNCTION: May cooperate with CD180 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) and cytokine production. Important for efficient CD180 cell surface expression (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space. Note=Associated with CD180 at the cell surface.


FUNCTION: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of UCS1025A, a member of the pyrrolizidinone family that acts as a strong telomerase inhibitor and displays potent antibacterial and antitumor properties (PubMed:29373009). These compounds share a hemiaminal-containing pyrrolizidinone core fused with a gamma-lactone, giving a furopyrrolizidine that is connected to a decalin fragment (PubMed:29373009). The polyketide synthase module (PKS) of the PKS-NRPS ucsA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:29373009). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with a 2S,3S-methylproline derived from L-isoleucine by the 2-oxoglutarate- dependent dioxygenase ucsF which converts L-isoleucine to (4S,5S)-4- methylpyrroline-5-carboxylate that is further converted to 2S,3S- methylproline by the pyrroline-5-carboxylate reductase ucsG (PubMed:29373009). Reductive release of the completed aminoacyl polyketide from the assembly line can form the 3-pyrrolin-2-one structure via an intramolecular Knoevenagel reaction (PubMed:29373009). Because ucsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ucsL (PubMed:29373009). This keto acyclic precursor is the substrate of the Diels-Alderase ucsH, that catalyzes the Diels-Alder cycloaddition (PubMed:29373009). Oxidation of the 3S-methyl group to a carboxylate by the cytochrome P450 monooxygenase ucsK allows an oxa-Michael cyclization that might involve the reductase/dehydrogenase ucsI and which furnishes the furopyrrolizidine (PubMed:29373009). The oxidase ucsJ likely plays a critical role in stereoselective reduction of the C5-C6 double bond to afford the required R-configured carboxylate group (Probable). Further enolization and oxidation at C5 by an unidentified enzyme affords the last intermediate that can undergo oxa-Michael cyclization to yield UCS1025A (Probable). SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.


FUNCTION: Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing (By similarity). This toxin is only active against insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.


FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylosuccinate synthetase family.


FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanB family. SIMILARITY: Belongs to the PanB family.


FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity). SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I NdhM subunit family.


FUNCTION: Induces low levels of natural DNA uptake by inducing transcription of the competence genes (the CRP-S regulon) required for DNA transformation. Induction of the CRP-S regulon also requires Sxy- activated promoter (CRP-S), cAMP receptor protein (CRP) and cAMP (PubMed:17068078, PubMed:22532864). Induces CRP-S site-containing genes which are involved in genome maintenance and transcription or encoding transposases and toxin-antitoxin pairs (PubMed:19502395). SIMILARITY: Belongs to the TfoX family.


FUNCTION: Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.


FUNCTION: May be involved in the development of the central nervous system. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Bicoid subfamily.


FUNCTION: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1 (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the dph1 subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.


FUNCTION: Binds and inhibits the conjugation of the ubiquitin-like G1P2/ISG15 protein to its target proteins. Since G1P2/ISG15 is an early antiviral protein, NS1 may inhibit the host antiviral response. Prevents EIF2AK2/PKR activation, either by binding double strand RNA or by interacting directly with EIF2AK2/PKR. Also binds poly(A) and U6 snRNA. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the influenza B viruses NS1 family.


FUNCTION: Oxygen-binding protein. May be involved in a storage mechanism or for delivery to oxygen-requiring enzymes. The oxygen- binding site contains two iron atoms. SIMILARITY: Belongs to the hemerythrin family.


SIMILARITY: Belongs to the DEPDC7 family.


FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CAF1 family.


FUNCTION: Plays a role in nitrite reduction. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: Shows antifungal activity towards B.cinerea and towards the wheat-specific pathogenic fungi F.culmorum and F.graminearum (groups 1 and 2).


FUNCTION: Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Cell projection, filopodium Cytoplasm, cell cortex Cell projection, microvillus Note=Colocalizes with F-actin in filopodia, cellular cortex and microvilli of the apical cell surface.


FUNCTION: PsaD can form complexes with ferredoxin and ferredoxin- oxidoreductase in photosystem I (PS I) reaction center. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the PsaD family.


FUNCTION: This protein may function to deliver copper to tyrosinase. SIMILARITY: Belongs to the melC1 family.


FUNCTION: Involved in rRNA-processing at A0, A1 and A2 sites and regulates negatively telomerase. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the PINX1 family.


FUNCTION: Multifunctional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles (By similarity). Required both to stabilize the assembly of the exocyst complex and to localize functional exocyst complexes to the leading edge of migrating cells (By similarity). Required for suppression of apoptosis (By similarity). In late stages of cytokinesis, upon completion of the bridge formation between dividing cells, mediates exocyst recruitment to the midbody to drive abscission (By similarity). Involved in ligand-dependent receptor mediated endocytosis of the EGF and insulin receptors (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Midbody Note=During late cytokinesis, enriched at the midbody. SIMILARITY: Belongs to the small GTPase superfamily. Ras family.


FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Exhibits high acyl-CoA specificity for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA (22:6-CoA, DHA-CoA) (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.


FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. 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). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ataxin-7 family.


FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.


FUNCTION: Maternal factor that plays a role in epigenetic chromatin reprogramming during early development of the zygote. Involved in the regulation of gametic DNA demethylation by inducing the conversion of the modified genomic base 5-methylcytosine (5mC) into 5- hydroxymethylcytosine (5hmC). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes in female and male zygote pronucleus. Associates preferentially with the paternal chromatin during zygote development.


FUNCTION: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PCNA family.


FUNCTION: Transcription factor playing important roles in primary neurulation and in the differentiation of stratified epithelia of both ectodermal and endodermal origin. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily.


FUNCTION: Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha- ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L- proline betaine. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family.


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


FUNCTION: May act as a membrane anchor for the chloroethene reductive dehalogenase VcrA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PceB family.


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


FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SIMILARITY: Belongs to the ChlB/BchB/BchZ family.


FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the cytoplasm, affects both translation and mRNA decay. Inhibits the polyadenylated RNA degradation by the Rrp41p 3'-->5' exonuclease in vitro. Binds with the 5'UTRs of PAB2, PAB3 and with a lower affinity with the 5'UTR of PAB5. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.


FUNCTION: Voltage-gated sodium channel Nav1.7/SCN9A inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 22 (Htx-4) subfamily.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eS6 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 family.


FUNCTION: Required for the timely initiation of chromosomal replication via direct interactions with the DnaA initiator protein. SIMILARITY: Belongs to the SIS family. DiaA subfamily.


FUNCTION: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. SIMILARITY: Belongs to the Lederbergvirus large terminase family.


FUNCTION: Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response. Initiates the repair of double-strand DNA breaks: recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins. Serine ADP-ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. HPF1 acts by completing the active site of PARP1 and PARP2: forms a composite active site composed of residues from HPF1 and PARP1 or PARP2. While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains. HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1. SUBCELLULAR LOCATION: Chromosome Nucleus Note=Localizes to DNA damage sites; chromatin localization is dependent on PARP1 and PARP2. SIMILARITY: Belongs to the HPF1 family.


FUNCTION: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GcdB/MmdB/OadB family.


FUNCTION: Heterodimer: MitTx, a heteromeric complex between Kunitz- and phospholipase-A2-like proteins, potently, persistently and selectively activates rat and chicken acid-sensing ion channel ASIC1 (PubMed:22094702, PubMed:24507937). Both alternatively spliced rat isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 nM) vs ASIC1b (EC(50)=23 nM) (PubMed:22094702). The rat ASIC3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM) (PubMed:22094702). On rat ASIC2a, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality (PubMed:22094702). Moderate and weak activations are also observed on the heterotrimers Asic1a-Asic2a and Asic1a-Asic3 (expressed in CHO cells), respectively (PubMed:22094702). The binding sites of the beta subunit of MitTx and the spider psalmotoxin-1 toxin overlap, explaining why these toxins are mutually exclusive (PubMed:22094702, PubMed:24507937). In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibers (PubMed:22094702). FUNCTION: Monomer: does not have phospholipase A2 activity but may maintain some lipid-binding character from its PLA2 lineage, which could aid in effecting neuronal depolarization. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. K49 sub-subfamily.


FUNCTION: Acts as a transcriptional regulator (By similarity). Mediates the differentiation of V2a interneurons (By similarity). Plays a role in eye development and organization of the neuroretina (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family.


FUNCTION: Probable tRNA nucleus export receptor which regulates tRNA processing and facilitates tRNA translocation across the nuclear pore complex. Is required for proper activity of the shoot apical meristem (SAM) and correct leaf initiation at different developmental stages, and may play a role in floral patterning. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the exportin family.


FUNCTION: Binds to GC box promoters elements and selectively activates mRNA synthesis from genes that contain functional recognition sites. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.


FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA subfamily.


FUNCTION: Does not seem to be a permease of pimelate. Its role in biotin synthesis is not clear. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: May control the transcriptional activity of MYC. Stimulates the activation of E box-dependent transcription by MYC. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. Note=Translocates into the nucleus in the S phase of the cell cycle upon an increase of MYC expression. Found in the mitochondria when associated with AKAP1. SIMILARITY: Belongs to the AMY1 family.


SIMILARITY: Belongs to the UbiD family.


FUNCTION: The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. SIMILARITY: Belongs to the shikimate dehydrogenase family.


FUNCTION: Terminal reductase that allows anaerobic growth on selenate as the sole respiratory oxidant. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.


FUNCTION: Attaches the circulating virion to the bacterial lipopolysaccharides which serve as receptor for the virus. Determines the phage host-range. Probably triggers with protein H the injection of the phage DNA into the host cytoplasm upon conformational changes induced by the interaction with host lipopolysaccharides (By similarity). SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the microvirus G protein family.


FUNCTION: Catalyzes the deimination of arginine residues of proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein arginine deiminase family.


FUNCTION: Involved in the transport of maltose and maltodextrins. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family. SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family.


FUNCTION: May act as a transcriptional activator or repressor. Involved in neurogenesis. Involved in the development of rhombomeres (r) 5 and 6 segments from their common precursor 'proto-segment' in the hindbrain. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Maf subfamily.


FUNCTION: Electron donor. Binds one copper ion. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.


FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Seems to participate in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for the Fe-S core formation. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the chlamydial CPn_0593/CT_474/TC_0759 family.


FUNCTION: May be a transcription factor with important functions in eye and nasal development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family.


FUNCTION: Inhibits antiviral activity induced by type I interferons. Does not block signal transduction of IFN, but is important to counteract the host antiviral state induced by a pre-treatment with IFN (By similarity). SIMILARITY: Belongs to the orthopoxvirus OPG027 family.


FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes (PubMed:18452584). Probably by regulating cGMP levels, required for activation of gametogenesis (PubMed:18452584). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.


FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily.


SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass membrane protein Host endosome membrane; Single-pass membrane protein.


FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family.


FUNCTION: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the inositol monophosphatase superfamily.


FUNCTION: Encapsidates the viral genome into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. Plays a role in protection of the genome from degradation, virus acquisition and transmission by insect vectors, infectivity, and systemic movement. The CP of monopartite geminiviruses is absolutely essential for virus movement (By similarity). SUBCELLULAR LOCATION: Virion Host nucleus. Note=It is actively transported into the host cell nucleus. It may be exported out of the nucleus through a nuclear export signal for cell-to-cell movement and spread (By similarity). SIMILARITY: Belongs to the geminiviridae capsid protein family.


FUNCTION: Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein (By similarity). SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.


SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CIA30 family.


FUNCTION: Involved in mercuric transport. Passes a mercury ion from the MerP protein to the mercuric reductase MerA. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity). SIMILARITY: Belongs to the trehalose phosphatase family.


SIMILARITY: Belongs to the FAM25 family.


FUNCTION: Guanylyltransferase that catalyzes the activation of (2S)-2- phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor. SIMILARITY: Belongs to the CofC family.


FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane protein; Lumenal side Lysosome lumen Cell membrane Cytoplasmic vesicle Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. SIMILARITY: Belongs to the glycosyl hydrolase 33 family.


FUNCTION: Probable serine-threonine kinase that may regulate brassinosteroid signaling. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. GSK-3 subfamily.


FUNCTION: Internal peptide VII: Cleavage product of Gp22 that is incorporated into the mature phage head. FUNCTION: Gp22 functions in head assembly.


FUNCTION: Inhibitor of HGF activator. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Plays essential roles both in the entry of the viral genome into the bacterial host and in budding process. The formation of the G3P-G6P complex termed adsorption complex is essential for correct termination of filamentous phage assembly (By similarity). SUBCELLULAR LOCATION: Virion Host membrane; Multi-pass membrane protein Note=Prior to assembly, G6P is found associated with the bacterial host inner membrane. There are about five copies of G6P in the mature virion. They are located together with G3P at the head side of the filamentous virion (By similarity). SIMILARITY: Belongs to the inovirus G6P protein family.


FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FrvAB PTS system is involved in fructose transport. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PEP-utilizing enzyme family.


FUNCTION: Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576. FUNCTION: Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576 (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.


FUNCTION: Catalyzes the condensation of (R)-4-phosphopantoate and beta- alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway. SIMILARITY: Belongs to the archaeal phosphopantothenate synthetase family.


FUNCTION: Low-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Trehalose transporter subfamily.


FUNCTION: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens (PubMed:23679205). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (+)-alpha-pinene (PubMed:23679205). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.


SIMILARITY: Belongs to the HupF/HypC family.


SIMILARITY: In the N-terminal section; belongs to the protein kinase superfamily. Ser/Thr protein kinase family. SIMILARITY: In the C-terminal section; belongs to the PP2C family.


FUNCTION: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7- deazaguanine (CDG), a step common to the biosynthetic pathways of all 7-deazapurine-containing compounds. SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7- deazaguanine synthase family.


FUNCTION: Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RIC family. YtfE subfamily.


FUNCTION: Catalyzes the cyclization of squalene into hopene. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the terpene cyclase/mutase family.


FUNCTION: Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Also plays a role in host immune evasion by inhibiting the host complement cascade activation (By similarity). FUNCTION: Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Also plays a role in host immune evasion by inhibiting the host complement cascade activation. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the herpesviridae glycoprotein C family.


FUNCTION: Involved in oxidative stress resistance. SIMILARITY: Belongs to the IprA family.


SIMILARITY: To Anabaena PCC 7120 alr2406.


FUNCTION: Functions in the pathway of anaerobic degradation of trihydroxybenzenes by catalyzing reduction of the aromatic nucleus prior to ring fission.


SIMILARITY: Belongs to the protein prenyltransferase subunit alpha family.


SUBCELLULAR LOCATION: Host membrane; Multi-pass membrane protein Virion. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CNTF family.


FUNCTION: Positive regulator of glutamate biosynthesis (gltAB genes). Negatively regulates its own expression. SIMILARITY: Belongs to the LysR transcriptional regulatory family.


FUNCTION: Probable metalloprotease. SIMILARITY: Belongs to the peptidase U62 family.


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


FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.


FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. SIMILARITY: Belongs to the poxviridae poly(A) polymerase catalytic subunit family.


FUNCTION: Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction. Appears to participate in the O-acetylation of GD3 ganglioside sialic acid. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Secreted Cytoplasmic vesicle, secretory vesicle, acrosome membrane; Peripheral membrane protein Note=Located in the acrosomal region of zona-pellucida bound sperm.


FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Nucleus. Note=Mitosis in the slime mold Plasmodium differs from the process in many eukaryotes. The tubulin chains must be transported to the nuclei for intranuclear assembly of the spindle. SIMILARITY: Belongs to the tubulin family.


FUNCTION: Facilitates protein transport into the nucleus. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family. KefB subfamily.


FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein. FUNCTION: Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site. SUBCELLULAR LOCATION: Virion Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. SIMILARITY: Belongs to the Leviviricetes capsid protein family.


FUNCTION: Plays a role in the negative regulation of NF-kappa-B signaling at the basal level by modulating transcriptional activity of NF-kappa-B on its target gene promoters. Associates with cyclin D1 promoter containing Myc E-box sequence and transcriptionally represses cyclin D1 expression. Regulates telomerase reverse transcriptase expression and telomerase activity in both ALT (alternative lengthening of telomeres)and telomerase-positive cell lines (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFS-II family. TFA subfamily.


SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the MAGUK family.


FUNCTION: First cyclic scorpion trypsin inhibitor (Kd~0.5 nM). Does not inhibit chymotrypsin. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Contributes to the expression of virulence factors and to pathogenicity via both agr-dependent and agr-independent pathways. Involved in the production of hemolysin, DNase, protease and protein A. Contributes to virulence in silkworm-infection model and murine model of systemic infection. FUNCTION: Contributes to the expression of virulence factors and to pathogenicity. Involved in the production of hemolysin, DNase, protease and protein A (By similarity). SIMILARITY: Belongs to the CvfB family.


FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA) and uses pyruvate or glyoxylate as amino-group acceptor. Cannot use beta-alanine, ornithine, acetylornithine, serine, glycine, asparagine, glutamine, glutamate, valine, leucine, isoleucine, methionine, phenylalanine, histidine, lysine, arginine, aspartate, threonine, tyrosine, tryptophan, proline, or cysteine as amino donors. Acts predominantly in vegetative tissues. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: GTPase-activating protein (GAP) with broad specificity. Acts as a GAP for RAB3A. Also exhibits significant GAP activity toward RAB22A, RAB27A, and RAB35 in vitro (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.


FUNCTION: Could be involved in the uptake of ribose. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GRP transporter (TC 2.A.7.5) family.


FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. FUNCTION: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme. SIMILARITY: Belongs to the RnpA family.


FUNCTION: Involved in the control of epidermal cell morphogenesis in petals. Promotes unidirectional cell expansion once outgrowth has been initiated (PubMed:17376813). Coordinately with WIN1/SHN1, participates in the regulation of cuticle biosynthesis and wax accumulation in reproductive organs and trichomes. Functions in cuticle nanoridge formation in petals and stamens, and in morphogenesis of petal conical cells and trichomes (PubMed:23709630). Functions as a major regulator of cuticle formation in vegetative organs by regulating the cuticle biosynthesis genes CYP86A8/LCR and CER1 (PubMed:24169067). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol in cholesterol biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family.


FUNCTION: Is involved in the reduction of 2,3- digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3- diphytanylglycerophospholipids (saturated archaeols) in the biosynthesis of archaeal membrane lipids. Catalyzes the formation of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di- O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of each double bond of the isoprenoid chains. SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL reductase subfamily.


FUNCTION: Diaminopimelinoyl-alanine endopeptidase. Has antibacterial activity. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Component of the PAF1 complex (PAF1C) which is involved in histone modifications such as methylation on histone H3 'Lys-4' (H3K4me3) (PubMed:20363855). Involved in regulation of flowering time. Required for the expression of the flowering repressor and MADS box gene FLC (PubMed:12207655). Involved in the control of seed dormancy and germination (PubMed:21799800). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the LEO1 family.


FUNCTION: Plays a role in odontogenesis. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: May participate in nuclear egress of viral particles. Plays a role in the dispersal of several host nucleolar proteins including NCL/nucleolin and NPM1. Since deletion of host NCL/nucleolin negatively impact on nuclear egress, UL24 supposedly acts on this process through its effect on host nucleoli (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm Host nucleus, host nucleolus Host Golgi apparatus. SIMILARITY: Belongs to the herpesviridae UL24 family.


FUNCTION: Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. SIMILARITY: Belongs to the 'phage' integrase family.


FUNCTION: Catalyzes the fourth and sixth steps in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. The C-terminus mediates the fourth step of the pathway and catalyzes the removal of UDP from C-1 of UDP-2,4-diacetamido-2,4,6- trideoxy-beta-L-altropyranose forming 2,4-diacetamido-2,4,6-trideoxy- beta-L-altropyranose. The N-terminal part mediates the last step of the pathway by mediating activation of pseudaminic acid with CMP by forming CMP-pseudaminic acid. SIMILARITY: In the N-terminal section; belongs to the CMP-NeuNAc synthase family. SIMILARITY: In the C-terminal section; belongs to the PseG family.


FUNCTION: Beta-glycosidase that catalyzes the transfer of glucose moiety to anthocyanidin 3-glucoside at the 7 position. Anthocyanins are ubiquitous colored pigments that are responsible for variations in petal color. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


FUNCTION: Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. FUNCTION: Metalloprotease that exhibits a cytotoxic effect leading to cell death. In host tissues, it could play a role in pathogenesis by modulating the stability of the extracellular matrix components such as fibronectin and fibrinogen. Also able to cleave plasminogen. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M6 family.


FUNCTION: Stabilizes the manganese cluster which is the primary site of water splitting (By similarity). Binds GTP after preillumination of photosystem II core complex. This binding is inhibited by DCMU. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane Note=Associated with the photosystem II complex. SIMILARITY: Belongs to the PsbO family.


FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione. SIMILARITY: Belongs to the Gfa family.


FUNCTION: May play a role in spermatogenesis. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SPATA31 family.


FUNCTION: Ubiquitin-like modifier protein which binds to a number of as yet unidentified target proteins. SIMILARITY: Belongs to the UFM1 family.


FUNCTION: Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)- acetylspermine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells. Also acts on 1,3- diaminopropane and 1,5-diaminopentane. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the acetyltransferase family.


FUNCTION: Required for primary cilia assembly. SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm. SIMILARITY: Belongs to the BBIP10 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uS11 family.


FUNCTION: Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Note=Associated with the kinetochore.


FUNCTION: Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto- oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box. SIMILARITY: Belongs to the MalT family.


FUNCTION: Part of the binding-protein-dependent transport system ModABCD for molybdenum; probably responsible for the translocation of the substrate across the membrane. FUNCTION: Part of the binding-protein-dependent transport system ModABCD for molybdenum; probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.


FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormone required for the initiation of metamorphosis. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Ras family.


FUNCTION: Involved in regulation of mitochondrial membrane ATP synthase. Necessary for H(+) conduction of ATP synthase. Facilitates energy-driven catalysis of ATP synthesis by blocking a proton leak through an alternative proton exit pathway. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane. SIMILARITY: Belongs to the ATP synthase subunit s family.


FUNCTION: 5-phosphoribose 1-diphosphate synthase involved in nucleotide, histidine, and tryptophan biosynthesis. Active in heteromultimeric complexes with other 5-phosphoribose 1-diphosphate synthases (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.


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


FUNCTION: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center of the complex close to the lumenal surface (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the SPCS3 family.


FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 25 (ICK4) subfamily.


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


FUNCTION: subunit of the RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs. SUBCELLULAR LOCATION: Virion. Host nucleus. SIMILARITY: Belongs to the influenza viruses PB2 family.


FUNCTION: A highly abundant outer membrane lipoprotein that controls the distance between the inner and outer membranes. The only protein known to be covalently linked to the peptidoglycan network (PGN). Also non-covalently binds the PGN. The link between the cell outer membrane and PGN contributes to maintenance of the structural and functional integrity of the cell envelope, and maintains the correct distance between the PGN and the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side Secreted, cell wall; Peptidoglycan-anchor Note=Attached via its lipidated N- terminus to the inner leaflet of the outer membrane. Attached to the peptidoglycan network (PGN) via its C-terminus. SIMILARITY: Belongs to the Lpp family.


FUNCTION: Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present. SIMILARITY: Belongs to the LutB/YkgF family.


FUNCTION: Seems to play a role in the dimerization of PSII. FUNCTION: Seems to play a role in the dimerization of PSII. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbT family. SIMILARITY: Belongs to the PsbT family.


FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EAF1 family.


FUNCTION: Plays a role in the regulation of lipogenesis, especially in lactating mammary gland. Important for the biosynthesis of triglycerides with medium-length fatty acid chains. May modulate lipogenesis by interacting with MID1IP1 and preventing its interaction with ACACA. May function as transcriptional coactivator. May modulate the transcription factor activity of THRB (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the SPOT14 family.


FUNCTION: [Isoform C]: Determines the expression of the blood group I antigen in erythrocytes. FUNCTION: Branching enzyme that converts linear into branched poly-N- acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 14 family.


FUNCTION: Mediates bacterial resistance to kanamycin, gentamicin, dibekacin, sisomicin, neomycin and tobramycin by adenylating the 2''- hydroxyl group of these antibiotics.


FUNCTION: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site (By similarity). SUBCELLULAR LOCATION: Cytoplasm Rough endoplasmic reticulum Note=Localizes exclusively with the rough reticulum endoplasmic (RER).


SIMILARITY: Belongs to the UPF0512 family.


FUNCTION: Promotes activation of caspases and apoptosis. Promotes mitochondrial membrane changes and efflux of apoptogenic proteins from the mitochondria. Contributes to p53/TP53-dependent apoptosis after radiation exposure. Promotes proteasomal degradation of MCL1. Competes with BAK1 and with BIM/BCL2L11 for binding to MCL1; can displace BAK1 and BIM/BCL2L11 from their binding sites (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the PMAIP1 family.


FUNCTION: Catalyzes the CoA- and ATP-dependent conversion of sulfoacetate to sulfoacetyl-CoA and AMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Antimicrobial peptide that potently inhibits growth of Mycobacterium tuberculosis (H37Rv strain) (MIC=3 uM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin I1 superfamily.


FUNCTION: Promotes actin polymerization mediated by SNX9 and WASL. SUBCELLULAR LOCATION: Cytoplasm Perikaryon Cell projection Cytoplasmic vesicle Note=Detected on neuronal cell bodies and cell projections, in part on cytoplasmic vesicles.


FUNCTION: 3'-to-5'exoribonuclease that preferentially degrades DNA and RNA oligonucleotides composed of only two nucleotides (By similarity). Binds and degrades longer oligonucleotides with a lower affinity (By similarity). Plays dual roles in mitochondria, scavenging nanoRNAs (small RNA oligonucleotides of <5 nucleotides) that are produced by the degradosome and clearing short RNAs that are generated by RNA processing (By similarity). Essential for correct initiation of mitochondrial transcription, degrading mitochondrial RNA dinucleotides to prevent RNA-primed transcription at non-canonical sites in the mitochondrial genome (By similarity). Essential for embryonic development (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Mitochondrion matrix Mitochondrion Cytoplasm Nucleus. SIMILARITY: Belongs to the oligoribonuclease family.


FUNCTION: Cell surface beta-glucosidase involved in cell wall biogenesis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the SUN family.


FUNCTION: Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1. Part of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. May act by regulating the GPI-GNT complex. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DPM2 family.


FUNCTION: Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. DDX15/PRP43 sub-subfamily.


FUNCTION: Antibacterial and antifungal activity. Presents chitin- binding activity (By similarity). SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Cytoplasmic granules of hemocytes and to a lesser extent in small granules of hemocytes. SIMILARITY: Belongs to the penaeidin family.


FUNCTION: Functions with VOA1 in assembly of the integral membrane sector (also called V0 sector) of the V-ATPase in the endoplasmic reticulum. Escorts the assembled V0 sector in COPII vesicles. Also required for normal packaging of the SNARE BOS1 and possibly the ER to Golgi transport receptor ERV29. FUNCTION: Functions with VOA1 in assembly of the integral membrane sector (also called V0 sector) of the V-ATPase in the endoplasmic reticulum. Escorts the assembled V0 sector in COPII vesicles. Also required for normal packaging of the SNARE BOS1 and possibly the ER to Golgi transport receptor ERV29. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the VMA21 family.


FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins (PubMed:21074048, PubMed:25103237, PubMed:26829768, PubMed:29593216). Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein (PubMed:21074048, PubMed:25103237). Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate (PubMed:25103237). Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK (PubMed:21074048). Mediates the deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation (PubMed:26829768). Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis (PubMed:29593216). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Golgi apparatus Cytoplasm, cytoskeleton, cilium basal body Note=Colocalizes with gamma- tubulin in the centrioles at interphase and dividing cells and with glutamylated tubulin in basal bodies of ciliated cells. SIMILARITY: Belongs to the peptidase M14 family.


FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. Specifically modifies U16 in tRNAs. SIMILARITY: Belongs to the Dus family. DusC subfamily.


FUNCTION: Disulfide isomerase which catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds (By similarity). Associates with calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (By similarity). Association with calcitriol does not affect its enzymatic activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum Endoplasmic reticulum lumen Melanosome. SIMILARITY: Belongs to the protein disulfide isomerase family.


FUNCTION: Atypical MAPK protein that regulates several process such as autophagy, ciliogenesis, protein trafficking/secretion and genome integrity, in a kinase activity-dependent manner. Controls both, basal and starvation-induced autophagy throught its interaction with GABARAP, MAP1LC3B and GABARAPL1 leading to autophagosome formation, SQSTM1 degradation and reduced MAP1LC3B inhibitory phosphorylation. Regulates primary cilium formation and the localization of ciliary proteins involved in cilium structure, transport, and signaling. Prevents the relocation of the sugar-adding enzymes from the Golgi to the endoplasmic reticulum, thereby restricting the production of sugar- coated proteins. Upon amino-acid starvation, mediates transitional endoplasmic reticulum site disassembly and inhibition of secretion. Binds to chromatin leading to MAPK15 activation and interaction with PCNA, that which protects genomic integrity by inhibiting MDM2-mediated degradation of PCNA. Regulates DA transporter (DAT) activity and protein expression via activation of RhoA. In response to H(2)O(2) treatment phosphorylates ELAVL1, thus preventing it from binding to the PDCD4 3'UTR and rendering the PDCD4 mRNA accessible to miR-21 and leading to its degradation and loss of protein expression (By similarity). Also functions in a kinase activity-independent manner as a negative regulator of growth (PubMed:9891064). Phosphorylates in vitro FOS and MBP (PubMed:11875070). During oocyte maturation, plays a key role in the microtubule organization and mei- otic cell cycle progression in oocytes, fertilized eggs, and early embryos (By similarity). Interacts with ESRRA promoting its re-localization from the nucleus to the cytoplasm and then prevents its transcriptional activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body Cell junction, tight junction Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasmic vesicle, autophagosome Golgi apparatus Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle Note=Co-localizes to the cytoplasm only in presence of ESRRA. Translocates to the nucleus upon activation (By similarity). At prometaphase I, metaphase I (MI), anaphase I, telophase I, and metaphase II (MII) stages, is stably detected at the spindle (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.


FUNCTION: Catalyzes the conversion of aminoimidazole ribotide (AIR) to 5-hydroxybenzimidazole (5-HBI) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Is thus involved in the anaerobic biosynthesis of the benzimidazole lower axial ligand of the cobamide produced by G.metallireducens. SIMILARITY: Belongs to the ThiC family. 5-hydroxybenzimidazole synthase subfamily.


FUNCTION: May function as a neurotransmitter or modulator. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.


FUNCTION: Encapsidates the viral DNA into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. The CP of bipartite geminiviruses is not required for cell-to-cell or systemic movement. SUBCELLULAR LOCATION: Virion Host nucleus Note=It is actively transported into the host cell nucleus. It may be exported out of the nucleus through a nuclear export signal for cell-to-cell movement and spread (By similarity). SIMILARITY: Belongs to the geminiviridae capsid protein family.


FUNCTION: Involved in the biosynthesis of momilactone A and B phytoalexins. Catalyzes the conversion of syn-copalyl diphosphate to the phytoalexin precursor syn-pimara-7,15-diene. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the terpene synthase family.


FUNCTION: Metal-independent, broad-range acid phosphatase. Involved, either directly or indirectly, in the bidirectional transport of sterols between the endoplasmic reticulum and the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the phosphoglycerate mutase family.


FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.


FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1- phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (By similarity). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (By similarity). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (By similarity). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro- dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (By similarity). Has also an N-acylethanolamine hydrolase activity (By similarity). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (By similarity). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (By similarity). SUBCELLULAR LOCATION: Lysosome Secreted Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. SIMILARITY: Belongs to the acid ceramidase family.


FUNCTION: May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins. SIMILARITY: Belongs to the arrestin family.


FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.


FUNCTION: Transcription factor. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: A probable mono(ADP-ribosyl)transferase; it is not known which residue is targeted for ADP-ribosylation. Upon expression in yeast cells causes cell death. SUBCELLULAR LOCATION: Secreted.


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


FUNCTION: Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP. SUBCELLULAR LOCATION: Cytoplasm Nucleus Nucleus, nucleolus Note=Predominantly cytoplasmic, shuttles between the nucleus and the cytoplasm. SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. YchF/OLA1 subfamily.


FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. SIMILARITY: Belongs to the troponin C family.


FUNCTION: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'- phosphopantotheine (By similarity). Required for growth and persistence in mice (PubMed:27676316). FUNCTION: Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'- phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'- phosphopantotheine. SIMILARITY: In the C-terminal section; belongs to the PPC synthetase family. SIMILARITY: In the N-terminal section; belongs to the HFCD (homo- oligomeric flavin containing Cys decarboxylase) superfamily.


FUNCTION: Transfers a methyl group to 7-hydroxyls of the isoflavones daidzein, genistein and 6,7,4'-trihydroxyisoflavone. Can also methylate (+)6a-hydroxymaackiain with lower efficiency. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.


FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1 family proteins to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi- pass membrane protein Note=Enriched in the cortical ER. Concentrated in punctae along the ER tubules. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.


FUNCTION: ATP-dependent rRNA helicase required for pre-ribosomal RNA processing. Involved in the maturation of the 35S-pre-rRNA and to its cleavage to mature 18S rRNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3 subfamily.


SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. KIN-7 subfamily.


FUNCTION: Involved in the regulation of root growth. Involved in the suppression of the root bending in response to touch stimuli, gravity and light. Regulates negatively stimulus-induced root bending through inhibition of root tip rotation. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the serine esterase family.


FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. SUBCELLULAR LOCATION: Secreted Membrane Note=Associated to membranes via binding to ATP6AP2. SIMILARITY: Belongs to the peptidase A1 family.


FUNCTION: Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. SIMILARITY: Belongs to the transferase hexapeptide repeat family.


FUNCTION: Lacks ADP-ribosylation enhancing activity. SIMILARITY: Belongs to the small GTPase superfamily. Arf family.


FUNCTION: Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. TDG/mug family.


FUNCTION: This enzyme catalyzes carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism. It effectively catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D- alanyl electrophilic group of the standard tripeptide substrate N- alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolyzing penicillin into penicilloate at a very low rate. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M15 family.


SIMILARITY: Belongs to the UPF0354 family.


SIMILARITY: Belongs to the baculoviridae gp41 family.


FUNCTION: Monovalent cation channel required for maintenance of rapid intracellular calcium release. May act as a potassium counter-ion channel that functions in synchronization with calcium release from intracellular stores. SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane; Multi-pass membrane protein Nucleus membrane. SIMILARITY: Belongs to the TMEM38 family.


FUNCTION: Positively regulates the expression of 5 genes involved in the catabolism of certain amides (amdS), omega amino acids (gatA and gabA), and lactams (lamA and lamB) in the presence of omega amino acid inducers. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Catalyzes the transfer of a methyl group from AdoMet to arsenite, producing methylated arsenicals. Involved in the conversion of As(III) to a number of methylated products. Reduces the arsenic toxicity in the cell and may contribute to the global arsenic cycling. SIMILARITY: Belongs to the methyltransferase superfamily. Arsenite methyltransferase family.


FUNCTION: Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:30244831). In the RQC complex, required to promote formation of 'Lys-48'-linked polyubiquitin chains during ubiquitination of incompletely synthesized proteins by LTN1 (PubMed:30244831). Also acts as a transcriptional repressor: represses transcription of SRF in vitro and so may play a role in heart development (PubMed:16574069). May play a role in cell death control (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Mainly nuclear. SIMILARITY: Belongs to the TCF25 family.


FUNCTION: This RNase has marked specificity towards the 3' side of uridine nucleotides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pancreatic ribonuclease family.


FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermatoxin subfamily.


FUNCTION: Common subunit for the receptors for a variety of interleukins. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell surface. SIMILARITY: Belongs to the type I cytokine receptor family. Type 5 subfamily.


FUNCTION: Sensor kinase that senses the plastoquinone (PQ) redox state involved in stoichiometry adjustment of both photosystems (e.g. long- term adaptation via transcriptional regulation of reaction center genes of photosystems I and II) and state transitions (e.g. short-term adaptation involving reversible post-translational phosphorylation of light-harvesting complex II, LHC II), thus linking photosynthesis with gene expression in chloroplasts (PubMed:18632566, PubMed:22039472). Autophosphorylates, probably on a tyrosine residue (PubMed:18632566). Probably phosphorylates SIGA/SIG1 in response to plastoquinone redox state modification (PubMed:23754813). Reduced PQ suppresses its autophosphorylation activity. Represses expression of a number of chloroplast-encoded genes (PubMed:31925322). SUBCELLULAR LOCATION: Plastid, chloroplast stroma Note=Associates with thylakoid membranes. SIMILARITY: Belongs to the chloroplast sensor kinase protein family.


FUNCTION: Putative antitoxin component of a possible type II toxin- antitoxin (TA) system. The cognate toxin is VapC23.


FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family.


FUNCTION: Anticodon endonuclease (ACNase) that triggers the cleavage ligation of tRNA(Lys). It is activated by T4 stp protein and masked by the prrD protein (the endonuclease subunit of EcoprrI) (PubMed:1691706). The prr locus restricts phage T4 mutants lacking polynucleotide kinase or RNA ligase; T4 mutants lacking these genes manifest a T4-induced anticodon nuclease (ACNase). It is thought that Stp and other T4-encoded ACNase factors counteract the masking agents, thus activating the latent ACNase (Probable).


FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C- terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane. SIMILARITY: Belongs to the polyomaviruses capsid protein VP2 family.


FUNCTION: Polymerase responsible for protein-primed viral DNA replication by strand displacement with high processivity and fidelity (By similarity). To start replication, the DNA polymerase forms a heterodimer with a free primer terminal protein (TP), recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP (PubMed:23110220). This polymerase possesses three enzymatic activities: DNA synthesis (polymerase), primer terminal protein (TP) deoxynucleotidylation, which is the formation of a covalent linkage (phosphoester) between the hydroxyl group of a specific serine residue in TP and 5'-dAMP, a reaction directed by the third T at the 3' end, and 3' to 5' exonuclease activity (PubMed:23110220, PubMed:19011105). Exonuclease activity has a proofreading purpose (By similarity). Since the polymerase initiates the replication on the third thymine, the TP- dAMP initiation product translocates backwards to recover the template information of the 2 terminal nucleotide (sliding back-mechanism) (PubMed:23110220, PubMed:19011105). SIMILARITY: Belongs to the DNA polymerase type-B family.


FUNCTION: Antimicrobial peptide. Has activity against the Gram-positive bacterium S.aureus (MIC=6 uM) and the Gram-negative bacterium E.coli (MIC=3 uM). Lacks hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.


SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the AATF family.


FUNCTION: Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1- phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose (PubMed:12473104, PubMed:27513637). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to D-glucose 6- phosphate (Glc-6-P) to form trehalose-6-phosphate (PubMed:12473104). Is specific for the glucosyl acceptor (Glc-6-P cannot be replaced by either mannose-6-P, fructose-6-P or glucosamine-6-P), but any of the glucose sugar nucleotides can be used as glucosyl donors (PubMed:12473104). It is more active with the purine sugar nucleotides than with the pyrimidine sugar nucleotides (PubMed:12473104). FUNCTION: Probably involved in the osmoprotection via the biosynthesis of trehalose and in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P). Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Probably also able to use ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc as glucosyl donors. SIMILARITY: Belongs to the glycosyltransferase 20 family. SIMILARITY: Belongs to the glycosyltransferase 20 family.


SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.


SIMILARITY: Belongs to the UPF0367 family.


FUNCTION: Has antifungal activity against P.infestans.


FUNCTION: Forms a fork protection complex (FPC) with tof1 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CSM3 family.


FUNCTION: Catalyzes the first step in biosynthesis of glycosaminoglycan. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein. Initial enzyme in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans in fibroblasts and chondrocytes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT subfamily.


FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.


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


SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.


FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9 subfamily.


FUNCTION: Symporter that transports one amino acid molecule together with two sodium and one chloride ions in kidneys and plays a role in the neutral amino acids reabsorption (PubMed:19478081, PubMed:26240152, PubMed:20377526). Preferentially transports neutral amino acids such as L-glycine and L-alanine but also other neutral amino acids (PubMed:19478081, PubMed:26240152, PubMed:20377526). Required CLTRN for cell surface expression and for its amino acid transporter activity (PubMed:26240152, PubMed:20377526). The transport mechanism is pH- independent (PubMed:19478081). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=In kidneys localizes to the apical membrane in distal segments of the proximal tubule (PubMed:19478081, PubMed:20377526). Cell membrane expression is CLTRN-dependent (PubMed:20377526). SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family. SLC6A18 subfamily.


FUNCTION: Positive regulator of hypersensitive response (HR)-like cell death. May be involved in potassium ion channel regulation.


FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. FUNCTION: Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function. SIMILARITY: Belongs to the CKS family.


FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Functions as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro- adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells (By similarity). Induces the formation of apical actin-dependent microvilli. SUBCELLULAR LOCATION: Apical cell membrane Cell projection, microvillus Membrane raft Cell projection, lamellipodium Cell projection, filopodium Cell projection, ruffle Membrane; Single- pass type I membrane protein Note=In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with NHERF2 at the apical plasma membrane during epithelial polarization. Colocalizes with NHERF1 at the trans-Golgi network (transiently). Its association with the membrane raft is transient. Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with actin filaments, ezrin and NHERF1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with EZR and NHERF2 at the apical cell membrane of glomerular epithelium cells (By similarity). Colocalizes with NHERF1 at the apical cell membrane. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis (By similarity). SIMILARITY: Belongs to the podocalyxin family.


FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. SUBCELLULAR LOCATION: Mitochondrion Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. SIMILARITY: Belongs to the universal ribosomal protein uL11 family.


FUNCTION: Lethal toxin which possesses an inhibitory effect on direct electrical stimulation of the isolated hemi-diaphragm of mice. Neither hemorrhagic nor hemolytic activities are detected. Phospholipase A2 activity, proteolytic activity and arginine esterolytic activity are absent (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family. Helofensin subfamily.


FUNCTION: Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore Note=Associated with kinetochores. SIMILARITY: Belongs to the NDC80/HEC1 family.


FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Shares much functionality with wnt11b. Signals through a non-canonical Wnt pathway to activate Jun-N- terminal kinase (JNK) to regulate gastrulation movements. Acts in a non-cell-autonomous manner to control neural crest migration, probably acting as an extracellular signal from surrounding tissue, but is not required for neural crest induction. Acts redundantly with wnt11b during pronephros induction. Regulates cardiac morphogenesis through the activation of JNK, but is not required for cardiac differentiation. Essential for dorsal fin development; required for an epithelial to mesenchymal transformation event prior to migration of cells into the fin, and ultimately for maintenance of fin structure. Mediates dorsal fin development through a non-canonical pathway mediated by Ca(2+). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family.


FUNCTION: Transcriptional activator that induces expression of multiple genes including pax3, en2, snai2/slug, feb and a subset of wnt genes. Has multiple key roles in the regulation of neural induction and neurogenesis: acts as a neural competence factor, sensitizing the presumptive neuroectoderm to respond to subsequent neuralizing signals. Promotes both preplacodal cell fates and neural crest cell fates, two of the cell populations that arise from the neural plate border. Cooperates with pax3 in concert with wnt signaling to determine neural crest fate. Synergizes with the bmp-inhibitor noggin/nog and acts through the wnt pathway to induce expression of en2. May bind to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.


FUNCTION: Innate immune adapter that mediates the recruitment and activation of IRF5 downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9. Following recruitment to endolysosome by SLC15A4 downstream of TLR7, TLR8 and TLR9, specifically recruits IRF5 transcription factor via its pLxIS motif, leading to IRF5 activation and subsequent expression of type I interferons. Plays a role in the regulation of endolysosomal pH in immune cells such as B-cells, dendritic cells and monocytes. SUBCELLULAR LOCATION: Lysosome membrane Endosome membrane Nucleus Cytoplasm Note=Recruited to endolysosome following interaction with SLC15A4. May colocalize with TLR7 in the endosomal pathway.


FUNCTION: Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the TPP enzyme family.


FUNCTION: Metalloproteinase inhibitor that acts on both matrix metalloproteinases Mmp1 and Mmp2 in vitro (PubMed:14567681). Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor (By similarity). Required for wing maturation which is the final step in morphogenesis of the adult fly (PubMed:16962574). Involved in the negative regulation of developmental tissue invasion for imaginal disk eversion during metamorphosis by inhibiting Mmp-mediated basement membrane (BM) degradation (PubMed:17301221). Required for oogenesis and for the long-term maintainance of germarial structure and shape in the adult ovaries. Required for maintaining composition and biophysical properties of the extracellular matrix (ECM), and for the normal organization and cyst production of the germline stem cell (GSC) niche (PubMed:26808525). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.


SIMILARITY: Belongs to the dynein light chain Tctex-type family.


FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins (PubMed:23891004). As a CIA complex component and in collaboration with CIAO1 specifically matures ACO1 and stabilizes IREB2 (PubMed:23891004). May play a role in chromosome segregation through establishment of sister chromatid cohesion. May induce apoptosis in collaboration with APAF1 (PubMed:25716227). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MIP18 family.