SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PPase class C family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family.


SIMILARITY: Belongs to the UPF0127 family.


SIMILARITY: Belongs to the PPR family. PCMP-E subfamily.


SIMILARITY: Belongs to the acylphosphatase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the PRA-PH family. SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.


FUNCTION: F-box protein probably involved in ubiquitin conjugation pathway.


SIMILARITY: Belongs to the acetyltransferase family.


FUNCTION: Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (Lipid III), the third lipid-linked intermediate involved in ECA synthesis. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the glycosyltransferase 56 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.


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


FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome. SIMILARITY: Belongs to the archaeal DnaG primase family.


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


FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.


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


FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase family.


FUNCTION: Functions as a PqqA binding protein and presents PqqA to PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway. SIMILARITY: Belongs to the PqqD family.


SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone 8 toxin family.


FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.


FUNCTION: Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Interferes also with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation (By similarity). In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-10 family.


FUNCTION: Essential core component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. In the TIM22 complex, it constitutes the voltage-activated and signal-gated channel. Forms a twin-pore translocase that uses the membrane potential as external driving force in 2 voltage-dependent steps (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family.


SIMILARITY: In the C-terminal section; belongs to the HAD-like hydrolase superfamily. MasA/MtnC family. SIMILARITY: In the N-terminal section; belongs to the aldolase class II family. MtnB subfamily.


FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.


FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.


SIMILARITY: Belongs to the CbrA family.


FUNCTION: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. SIMILARITY: Belongs to the bacterial histone-like protein family.


FUNCTION: Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HSP33 family.


FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two- step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 2 subfamily.


FUNCTION: [Outer capsid protein VP8*]: Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. In some other strains, VP8* mediates the attachment to histo- blood group antigens (HBGAs) for viral entry. FUNCTION: [Outer capsid protein VP4]: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts. FUNCTION: [Outer capsid protein VP5*]: Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment. SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion Host rough endoplasmic reticulum Host cell membrane Host cytoplasm, host cytoskeleton Host endoplasmic reticulum-Golgi intermediate compartment Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple- layered particles. VP4 also seems to associate with lipid rafts of the host cell membrane probably for the exit of the virus from the infected cell by an alternate pathway. SUBCELLULAR LOCATION: [Outer capsid protein VP8*]: Virion Note=Outer capsid protein. SUBCELLULAR LOCATION: [Outer capsid protein VP5*]: Virion Note=Outer capsid protein. SIMILARITY: Belongs to the rotavirus VP4 family.


FUNCTION: Involved in the anomeric conversion of L-rhamnose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the rhamnose mutarotase family.


FUNCTION: Transcription factor that plays a role in the activation of archaeal genes transcribed by RNA polymerase. Facilitates transcription initiation by enhancing TATA-box recognition by TATA-box-binding protein (Tbp), and transcription factor B (Tfb) and RNA polymerase recruitment. Not absolutely required for transcription in vitro, but particularly important in cases where Tbp or Tfb function is not optimal. It dynamically alters the nucleic acid-binding properties of RNA polymerases by stabilizing the initiation complex and destabilizing elongation complexes. Seems to translocate with the RNA polymerase following initiation and acts by binding to the non template strand of the transcription bubble in elongation complexes. SIMILARITY: Belongs to the TFE family.


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


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase D subunit family.


FUNCTION: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the quinolinate synthase family. Type 1 subfamily.


FUNCTION: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, telomere. SIMILARITY: Belongs to the protein kinase superfamily. BUD32 family.


FUNCTION: A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family.


SIMILARITY: Belongs to the UPF0231 family.


FUNCTION: Binds 5S rRNA, forms part of the central protuberance of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL5 family.


FUNCTION: Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.


FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.


FUNCTION: Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family.


FUNCTION: Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5- deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP. SIMILARITY: Belongs to the CofD family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family. Venom allergen 5-like subfamily.


FUNCTION: Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane. Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate. Does not mediate fructose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Perikaryon Cell projection Note=Localized to densely spaced patches along neuronal processes. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL38 family.


SIMILARITY: Belongs to the DNA glycosylase MPG family.


FUNCTION: Seems to be required for the assembly of the photosystem I complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ycf4 family.


FUNCTION: Has bactericidal activity. Active against E.coli ML35 and S.aureus 502A. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: The antenna complex functions as a light receptor, it captures and delivers excitation energy to photosystems II and I. The Prochlorales pcb genes are not related to higher plant LHCs. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. IsiA/Pcb subfamily.


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


FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA subfamily.


FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side.


FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily.


FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids other than diacylglycerol (DAG). SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.


FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast.


FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.


FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP16 family.


FUNCTION: ATPase required for the post-translational delivery of tail- anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum Golgi apparatus Note=GET1 and GET2 are required for targeting GET3 to the endoplasmic reticulum. SIMILARITY: Belongs to the arsA ATPase family.


FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family.


FUNCTION: During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions. FUNCTION: During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the VPR carried into the virion. Additionally, VPR induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Detected in the serum and cerebrospinal fluid of AIDS patient, VPR may also induce cell death to bystander cells. SUBCELLULAR LOCATION: Virion Host nucleus Host extracellular space Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may function independently of the human importin pathway. Detected in high quantity in the serum and cerebrospinal fluid of AIDS patient. SIMILARITY: Belongs to the HIV-1 VPR protein family.


FUNCTION: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress. SIMILARITY: Belongs to the globin family. Two-domain flavohemoproteins subfamily. SIMILARITY: In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.


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


FUNCTION: Probable promoter-specific protein mediating the interaction between DNA and RNA polymerase. SUBCELLULAR LOCATION: Plastid, chloroplast.


FUNCTION: Catalyzes the specific phosphorylation of arginine residues in proteins. SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.


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


FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase VIIa family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL41 family.


FUNCTION: Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FdhD family.


FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin- independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host apical cell membrane; Single-pass type I membrane protein Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. SIMILARITY: Belongs to the influenza viruses hemagglutinin family.


FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.


SIMILARITY: Belongs to the UPF0229 family.


FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.


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


FUNCTION: Early transcription factor that plays a key role in somitogenesis, paraxial mesoderm development and regulation of stem cell pluripotency. Essential for the mesenchymal to epithelial transition associated with somite formation. Required for somite morphogenesis, thereby regulating patterning of the axial skeleton and skeletal muscles. Required for proper localization of somite epithelium markers during the mesenchymal to epithelial transition. Also plays a key role in regulation of stem cell pluripotency. Promotes pluripotency exit of embryonic stem cells (ESCs) by priming ESCs for differentiation. Acts as a key regulator of self-renewal of hematopoietic stem cells (HSCs) by mediating HSCs quiescence and long- term self-renewal. Together with MEOX2, regulates transcription in heart endothelial cells to regulate fatty acid transport across heart endothelial cells. Acts by forming a heterodimer with another helix- loop-helix (bHLH) protein, such as TCF3/E12, that binds DNA on E-box motifs (5'-CANNTG-3') and activates transcription of target genes. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the spermidine/spermine synthase family.


FUNCTION: Catalyzes the attachment of tryptophan to tRNA(Trp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.


SIMILARITY: Belongs to the UPF0213 family.


FUNCTION: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. SUBCELLULAR LOCATION: Cell outer membrane; Peripheral membrane protein. Note=Attached to the inner leaflet of the outer membrane. SIMILARITY: In the C-terminal section; belongs to the transglycosylase Slt family. SIMILARITY: In the N-terminal section; belongs to the bacterial solute- binding protein 3 family.


FUNCTION: Involved in the presentation of foreign antigens to the immune system. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the MHC class I family.


FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL- diaminopimelate. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. LL-diaminopimelate aminotransferase subfamily.


FUNCTION: Involved in cell division and chromosome segregation. SIMILARITY: Belongs to the WhiA family.


FUNCTION: Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B). SIMILARITY: Belongs to the anti-sigma-factor family.


FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.


FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C15 family.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family.


FUNCTION: Catalyzes the deformylation of 4-deoxy-4-formamido-L- arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose- phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (By similarity). Has anti- helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted from pancreatic acinar cells in its inactive form. SIMILARITY: Belongs to the phospholipase A2 family.


SIMILARITY: Belongs to the UPF0248 family.


SIMILARITY: Belongs to the class II ribonucleoside-triphosphate reductase family.


FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP4 may act as a sperm receptor. SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 4]: Zona pellucida. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the ZP domain family. ZPB subfamily.


FUNCTION: Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange. SIMILARITY: Belongs to the eukaryotic RecA-like protein family. RadB subfamily.


FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 13 family.


FUNCTION: Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of replication as well as for processivity of DNA replication. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the beta sliding clamp family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the heme-copper respiratory oxidase family.


FUNCTION: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. SIMILARITY: Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Cytoplasm. Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles. Also detected as large dots in the perinuclear region (By similarity). SIMILARITY: Belongs to the RMDN family.


FUNCTION: Involved in the catabolism of homogentisate (2,5- dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate. SIMILARITY: Belongs to the homogentisate dioxygenase family.


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


FUNCTION: Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8- hydroxy-5-deazariboflavin from 5-amino-5-(4-hydroxybenzyl)-6-(D- ribitylimino)-5,6-dihydrouracil. SIMILARITY: Belongs to the radical SAM superfamily. CofG family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M48B family.


FUNCTION: Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 08 (Shiva) family. 01 (omega toxin) subfamily.


SIMILARITY: Belongs to the UPF0346 family.


FUNCTION: Involved in the degradation of chitin. ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YdjC deacetylase family. ChbG subfamily.


FUNCTION: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CbiM family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family.


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


SIMILARITY: Belongs to the prokaryotic GSH synthase family.


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


FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PetN family.


SIMILARITY: Belongs to the ribulokinase family.


FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol. SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase family. TagBP aldolase GatY subfamily.


FUNCTION: A probable RNA-binding protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the KhpA RNA-binding protein family.


FUNCTION: Catalyzes the decarboxylation of oxaloacetate into pyruvate. Seems to play a role in maintaining cellular concentrations of bicarbonate and pyruvate. SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. Oxaloacetate decarboxylase family.


FUNCTION: ATP-dependent DNA helicase important for chromosome transmission and normal cell cycle progression in G(2)/M (By similarity). May have a role in changing DNA topology to allow the loading of proteins involved in maintaining sister chromatid cohesion in the vicinity of the centromeres (By similarity). Has a specific role in chromosome segregation during meiosis II (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily. DDX11/CHL1 sub-subfamily.


FUNCTION: This protein complexes cadmium, zinc and copper. SIMILARITY: Belongs to the metallothionein superfamily. Type 14 family.


SIMILARITY: Belongs to the methyltransferase superfamily.


FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family. Ribosome biogenesis protein NSA2 subfamily.


FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. Also exhibits THF-independent aldolase activity toward beta- hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family.


FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RuBisCO small chain family.


FUNCTION: Serine peptidase whose precise substrate specificity remains unclear (By similarity). Does not cleave peptides after a arginine or lysine residue (By similarity). Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex (By similarity). May play a role in the regulation of synaptic vesicle exocytosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus, trans-Golgi network Cytoplasm, cytoskeleton Golgi apparatus Nucleus Note=Co-localizes with AP-1 in the trans-Golgi network (By similarity). Co-localizes with MAP2 and ACTB on the cytoskeleton (By similarity). Co-localizes with STX6 and GOSR2 at the Golgi apparatus (By similarity). SIMILARITY: Belongs to the peptidase S9A family.


FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DapA family. NanA subfamily.


FUNCTION: May be involved in specific transport of UDP-Gal from the cytosol to the Golgi lumen. Involved in the maintenance of optimal conditions for the folding of secretory pathway proteins in the endoplasmic reticulum (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily.


FUNCTION: Required for cell viability in cells lacking mitochondrial DNA. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MGR2 family.


FUNCTION: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down- regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo. SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the HIV-1 VPU protein family.


SIMILARITY: Belongs to the UPF0125 (RnfH) family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein srd family.


FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism. SIMILARITY: Belongs to the GlnD family.


SIMILARITY: Belongs to the 14-3-3 family.


FUNCTION: Required for insertion of 4Fe-4S clusters. SIMILARITY: Belongs to the HesB/IscA family.


FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.


FUNCTION: Multidrug efflux pump. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.


FUNCTION: The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. SUBCELLULAR LOCATION: Cellular chromatophore membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily.


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


FUNCTION: Zeins are major seed storage proteins. SIMILARITY: Belongs to the zein family.


FUNCTION: Multifunctional RNA-binding protein that recognizes the K- turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.


SUBCELLULAR LOCATION: Spore core. SIMILARITY: Belongs to the SspH family.


FUNCTION: Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe(3+) into Fe(2+). It is also able to reduce extracellular monodehydro-L-ascorbate and may be involved in extracellular ascorbate regeneration (By similarity). May also function as a cupric transmembrane reductase (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein.


FUNCTION: Plays a role in skin pigmentation by antagonizing the action of melanotropin alpha. Induces melanin concentration within the melanophores. May participate in the control of the hypothalamo- pituitary adrenal gland axis by inhibiting the release of ACTH. SIMILARITY: Belongs to the melanin-concentrating hormone family.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 8 family.


FUNCTION: Required for growth under high-pressure and low-temperature conditions. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DLT1 family.


FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily.


FUNCTION: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ4 family.


FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA- DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery. SIMILARITY: Belongs to the hepadnaviridae P protein family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 24 kDa subunit family.


FUNCTION: May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the germin family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase protein 8 family.


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


FUNCTION: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP- binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide exporter (TC 3.A.1.122) family.


FUNCTION: Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity. SIMILARITY: Belongs to the DNA mismatch repair MutS family. MutS2 subfamily.


SIMILARITY: Belongs to the Smg family.


FUNCTION: The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Note=Cytoplasmic membrane (in a transfection system). SIMILARITY: Belongs to the beta type-B retroviral Gag protein family. HERV class-II K(HML-2) gag subfamily.


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


FUNCTION: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the protein disulfide isomerase family.


FUNCTION: Required for dimerization of active 70S ribosomes into 100S ribosomes in stationary phase; 100S ribosomes are translationally inactive and sometimes present during exponential growth. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HPF/YfiA ribosome-associated protein family. Long HPF subfamily.


FUNCTION: Potential calcium sensor. SIMILARITY: Belongs to the calmodulin family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cytidylate kinase family. Type 2 subfamily.


FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation- induced autophagy. Involved in correct ATG9 trafficking to the pre- autophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the WD repeat PROPPIN family.


FUNCTION: eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.


FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis. SUBCELLULAR LOCATION: Host cell membrane; Lipid-anchor; Cytoplasmic side Virion Secreted Host Golgi apparatus membrane Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. SIMILARITY: Belongs to the lentivirus primate group Nef protein family.


FUNCTION: This highly disulfide-bonded protein is a potent inhibitor of factor Xa. May have therapeutic utility as an anticoagulant. Also exhibits a strong metastatic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I15 (antistasin) family.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the complex I 23 kDa subunit family.


FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits (By similarity). FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. SIMILARITY: Belongs to the RNA polymerase subunit omega family. SIMILARITY: Belongs to the RNA polymerase subunit omega family.


FUNCTION: Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.


FUNCTION: Essential serine-protein kinase involved in the early stage of virion morphogenesis. SUBCELLULAR LOCATION: Host endoplasmic reticulum Host endoplasmic reticulum-Golgi intermediate compartment. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Poxviruses subfamily.


FUNCTION: Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side Note=Loosely associated with the cytoplasmic side of the inner membrane, probably via SecY. SIMILARITY: Belongs to the Syd family.


FUNCTION: Negatively regulates the transcription of the flagellar master operon flhDC by binding to the upstream region of the operon. SIMILARITY: Belongs to the LysR transcriptional regulatory family.


FUNCTION: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Thiamine importer (TC 3.A.1.19.1) family.


FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the 2-acyl-GPE acetyltransferase family. SIMILARITY: In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Binds and inhibits cysteine proteinases. Inhibits most strongly papain and cathepsin L, more weakly bromelain and cathepsin B while it is completely ineffective against cathepsin H. SUBCELLULAR LOCATION: Note=Not secreted. SIMILARITY: Belongs to the protease inhibitor I48 family.


FUNCTION: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA subfamily.


FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparing capsid uncoating. SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 2 family.


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


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.


FUNCTION: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase. SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae HEPA family.


FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D 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 L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the NifH/BchL/ChlL family.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrDE/RnfAE family.


FUNCTION: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the BamB family.


FUNCTION: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. May also be involved in early transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Note=Nuclear pore complex cytoplasmic fibrils. SIMILARITY: Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily.


FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin- independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host apical cell membrane; Single-pass type I membrane protein Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. SIMILARITY: Belongs to the influenza viruses hemagglutinin family.


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


FUNCTION: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. MAP kinase subfamily. HOG1 sub-subfamily.


FUNCTION: Involved in ribosomal large subunit assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RRS1 family.


FUNCTION: Catalyzes the facilitated diffusion of 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) into the cell. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. LplT (TC 2.A.1.42) family.


FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RraA family.


FUNCTION: Transforms N(2)-succinylglutamate into succinate and glutamate. SIMILARITY: Belongs to the AspA/AstE family. Succinylglutamate desuccinylase subfamily.


SIMILARITY: Belongs to the UPF0276 family.


SIMILARITY: Belongs to the GARS family.


SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


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


FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=Part of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family.


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


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UPF0298 family.


FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for piRNA biogenesis by facilitating loading of piRNAs into PIWI proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the heat shock protein 90 family.


FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the dethiobiotin synthetase family.


FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. SIMILARITY: In the C-terminal section; belongs to the precorrin methyltransferase family. SIMILARITY: In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.


FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3- phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid- dihydrodiol (CI-dihydrodiol), respectively. SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase beta subunit family.


FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the small Tim family.


FUNCTION: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins- secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). SUBCELLULAR LOCATION: Secreted Cell membrane.


FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta- barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MMM1 family.


FUNCTION: This protein binds specifically to 23S rRNA. FUNCTION: The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uL22 family.


FUNCTION: Secreted metalloproteinase probably acting as a virulence factor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M36 family.


FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the IPP isomerase type 1 family.


FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates. SIMILARITY: Belongs to the SsuD family.


FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.


FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II topoisomerase GyrB family.


FUNCTION: May act as a deubiquitinating enzyme.


FUNCTION: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Increases plasmodesma size exclusion limit. Acts as a suppressor of RNA-mediated gene silencing, also known as post- transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs (By similarity). SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the Tymovirales TGBp1 protein family.


FUNCTION: Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme. SIMILARITY: Belongs to the dynein light chain family.


FUNCTION: Activates expression of the rhaBAD and rhaT operons. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity). SIMILARITY: Belongs to the bacterial ribosomal protein bL20 family.


FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal tRNAs. SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.


FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the KdpA family.


SIMILARITY: Belongs to the carbohydrate kinase PfkB family.


FUNCTION: Probable transcriptional coactivator. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.


FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre- mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs (By similarity). SUBCELLULAR LOCATION: Host nucleus, host nucleolus. Host cytoplasm. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm.


FUNCTION: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. SIMILARITY: Belongs to the NMT1/THI5 family.


FUNCTION: Involved in rRNA processing. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the EFG1 family.


FUNCTION: Promotes transcriptional elongation by Su(Tpl)/ELL. Essential for development (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EAF family.


FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid. SUBCELLULAR LOCATION: Mitochondrion outer membrane. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO subfamily.


SIMILARITY: Belongs to the autoinducer-regulated transcriptional regulatory protein family.


FUNCTION: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. AraH/RbsC subfamily.


FUNCTION: This protein is an aporepressor. When complexed with L- tryptophan it binds the operator region of the trp operon (5'- ACTAGT-'3') and prevents the initiation of transcription. The complex also regulates trp repressor biosynthesis by binding to its regulatory region. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TrpR family.


SIMILARITY: Belongs to the WEB family.


SIMILARITY: Belongs to the TelA family.


FUNCTION: Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response', an adaptive process that allows bacteria to respond to amino acid starvation, resulting in the coordinated regulation of numerous cellular activities. SIMILARITY: Belongs to the GppA/Ppx family. GppA subfamily.


FUNCTION: DNA helicase which participates in several chromatin remodeling complexes, including the SWR1 and the INO80 complexes. The SWR1 complex mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. The INO80 complex remodels chromatin by shifting nucleosomes and is involved in DNA repair. Also involved in pre-rRNA processing (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RuvB family.


FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan, the main structural component of the cell wall. It could also function biosynthetically as a transglycosylase (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family.


FUNCTION: During stationary phase, binds the chromosome non- specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Dps family.


SIMILARITY: Belongs to the UPF0325 family.


FUNCTION: Regulates drug efflux through modulation of ABCB1 localization and activity. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.


FUNCTION: May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.


FUNCTION: Acts as a radical domain for damaged PFL and possibly other radical proteins.


FUNCTION: This insecticidal carbohydrate-binding lectin is toxic for the cowpea weevil. SIMILARITY: Belongs to the leguminous lectin family.


FUNCTION: May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota subfamily.


SIMILARITY: Belongs to the RimK family.


FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL5 family.


SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the asfivirus F317L family.


SIMILARITY: Belongs to the UPF0212 family.


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


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


FUNCTION: May function as histone H3 lysine demethylase and be involved in regulation of gene expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the JARID1 histone demethylase family.


FUNCTION: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Responsible for synthesis of pseudouridine from uracil-2605 in 23S ribosomal RNA. SIMILARITY: Belongs to the pseudouridine synthase RsuA family.


FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). Catalyzes the transfer of the gamma-phosphate group from ATP to the 1- hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. SIMILARITY: Belongs to the rhamnulokinase family.


FUNCTION: NADH-dependent reductase for dph3 and cytochrome b5. 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 reducing dph3, also involved in the formation of the tRNA wobble base modification mcm5s 2U (5-methoxycarbonylmethyl-2- thiouridine), mediated by the elongator complex. The cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.


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


FUNCTION: May play a structural or regulatory role in gas vesicle synthesis. SUBCELLULAR LOCATION: Gas vesicle.


FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.


SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the protein disulfide isomerase family.


FUNCTION: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle. SIMILARITY: Belongs to the aspartate/glutamate racemases family. ALMA1 subfamily.


FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily.


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


FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the MnmA/TRMU family.


FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family.


SIMILARITY: Belongs to the aldolase LacD family.


SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the PRRC1 family.


FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family.


SIMILARITY: Belongs to the GMC oxidoreductase family.


FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.


FUNCTION: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the P33MONOX family.


FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRF amide related peptide) family.


SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the HflD family.


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


FUNCTION: 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. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family.


FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To cation A.eutrophus efflux system protein CzcD.


FUNCTION: Specifically catalyzes the dephosphorylation of 2- phosphoglycolate. Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3'-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.


FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase A22B family.


FUNCTION: Catalyzes the two-electron reduction of the C2 and C3(1) diene system of 15,16-dihydrobiliverdin. SIMILARITY: Belongs to the HY2 family.