There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
Ribosomal protein L3-specific, glutamine-N5-methyltransferase
Type:
Family
Description:
This entry represents a protein-(glutamine-N5) methyltransferase, often annotated as PrmB or YfcB, which modifies ribosomal protein L3 [
]. It is closely related to HemK, the N(5)-glutamine methyltransferase for a critical residue in peptide release factors RF-1 and RF-2.
There is currently no experimental data to indicate the function of proteins in this family. Some family members appear to contain a merR-type HTH DNA-binding domain.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
This entry consists of the checkpoint protein Rad24 from budding yeast and its homologue, Rad17, from other organisms. This entry does not include Rad17 from plants. In Saccharomyces cerevisiae, Rad24 forms a complex with replication factor C (RFC) proteins, including Rfc2, Rfc3, Rfc4, and Rfc5. When DNA damage is detected, the Rad24-RFC complex loads Rad17-Mec3-Ddc1 complex onto chromatin and activates DNA damage checkpoint, which then leads to cell cycle arrest and DNA repair [
]. The Rad24-RFC complex is involved in both the mitotic and meiotic checkpoints []. Besides checkpoint activation, Rad24 is also involved in double-strand break ends processing, DNA repair and telomere maintenance [,
,
,
]. In human, the comparable DNA damage checkpoint components, Rad17 and the Rad1-Rad9-Hus1 (9-1-1) complex, play similar roles in DNA damage surveillance and checkpoint activation as their counter partners (Rad24, Rad17-Mec3-Ddc1) in budding yeast. Rad17 participates in the recruitment of the 9-1-1 complex onto chromatin. Besides checkpoint activation, Rad17 may also serve as a sensor of DNA replication progression, and may be involved in homologous recombination [
]. Overexpression of Rad17 has been associated with human breast and colon cancers [,
]. It's worth noting that the name, Rad17, has been used for different proteins in budding yeast and other organisms. In this entry, Rad17, is the homologue of the budding yeast Rad24 and has no homology with budding yeast Rad17
Rad52 was identified in Saccharomyces cerevisiae (Baker's yeast) as a component of the homologous recombination repair pathway and to play an important role in both meiotic and mitotic recombination. The human protein is highly homologous in both structure and function. In the presence of absence of DNA, Rad52 forms ring-shaped oligomers which bind both single and double stranded DNA, stimulating annealing of complimentary DNA strands and promoting ligation of both cohesive and blunt-end fragments. Rad52 may act as a recombination mediator, optimising catalysis of strand exchange by the Rad51 protein.A C-terminal self-association domain has been identified that mediates formation of higher order oligomers of Rad52 rings. Formation of these oligomers may be important for interaction with more than one DNA molecule [
].
Members of this family are paralogues to the authentic thiosulfate oxidation system protein SoxY. True SoxY end with the sequence GGCG(G), the swinging arm in which the Cys residue covalently binds the inorganic sulfur moiety. In this family, members end with a different swinging arm sequence, [AS]AC[IVT]E. The few species with a member of this family always have authentic SoxY [
].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. However, they are predicted to be integral membrane proteins (with several transmembrane segments). Homologues are predominantly from Actinobacteria.
A-kinase anchor protein 12 (AKAP12) is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC) [
]. AKAP12 may play a tumor/angiogenesis suppressor role [].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
Bardet-Biedl syndrome is a member of genetic ciliopathies, but the link between cilia/centrosome deficits and metabolic abnormalities is not completely clear [
]. Bardet-Biedl syndrome (BBS) is a heterogeneous genetic disorder characterised by many features, including retinal degeneration, obesity, cognitive impairment, polydactyly, renal abnormalities, and hypogenitalism. BBS genes play an important role in maintainingleptin sensitivity in proopiomelanocortin neurons [
]. A relatively high incidence of BBS is found in the mixed Arab populations of Kuwait and in Bedouin tribes throughout the Middle East, most likely due to the high rate of consaguinity in these populations and a founder effect.Primary cilia are ubiquitous cellular appendages that provide important sensory and signalling functions and their dysfunction underlies numerous human genetic disorders. The proteins disrupted in the human ciliary disorder Bardet-Biedl syndrome (BBS) are required for the localisation of G protein-coupled receptors to primary cilia on central neurons. The alteration of signalling caused by mislocalisation of ciliary signalling proteins underlies the BBS phenotype [
]. Of the 12 known BBS genes, BBS1 is the most commonly mutated [].This group represents a Bardet-Biedl syndrome 7 protein.
Mitochondrial ribosomal protein 63 is present in the intact 55S subunit of the mitochondrial ribosome. It is not known if it belongs to the 28S or to the 39S subunit [
].
DsbL is involved in disulfide-bond formation. It acts by transferring its disulfide bond to other proteins. DsbL, along with DsbI, form part of a redox system that mediates formation of an essential disulfide bond in ASST (uropathogen-specific arylsulfate sulfotransferase). DsbL and DsbI represent a second specific redox couple that guarantees biological activity of ASST [
].
This domain forms part of the integron cassette protein Hfx_CASS5 present in Vibrio cholerae. The structure of Hfx is a tetramer built from two domain-swapped dimers [
].
This entry represents lactate utilization protein B, which is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source [
]. It is thought to function as an electron transporter during oxidation of L-lactate.
This family represents one out of two closely related orthologous sets of proteins that, so far, are found only in but, are universal among, the Archaea.
This orthologue set includes MJ1210 from Methanocaldococcus jannaschii (Methanococcus jannaschii) and AF0525 from Archaeoglobus fulgidus, but not MJ0106 or AF1251. The proteins are of unknown function.
This entry represents Ribosomal protein S35, which localises to the mitochondria in live cells and co-fractionates with purified mitochondrial ribosomes. This group of proteins have a novel function in the control of cell respiration by acting on the mitochondrial protein synthesis machinery and a role in mitochondrial integrity. Observations also indicate that in Schizosaccharomyces pombe (Fission yeast), alterations of mitochondrial function are linked to changes in cell cycle and cell morphology control mechanisms [
].
This family consists exclusively of archaeal RadA protein, a homologue of bacterial RecA, eukaryotic RAD51 (
), and archaeal RadB (
). This protein is
involved in DNA repair and in homologous recombination, it binds and assembles on single-stranded DNA to form a nucleoprotein filament. RadA hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules involved in DNA repair and recombination. The member from Pyrococcus horikoshii contains an intein [].
This family of proteins represent HslU, a bacterial clpX homologue, which is an ATPase and chaperone belonging to the AAA Clp/Hsp100 family and a component of the eubacterial proteasome. ATP-dependent protease complexes are present in all three kingdoms of life, where they rid the cell of misfolded or damaged proteins and control the level of certain regulatory proteins. They include the proteasome in Eukaryotes, Archaea, and Actinomycetales and the HslVU (ClpQY, ClpXP) complex in other eubacteria. Genes homologous to eubacterial HslV,
, (ClpQ,) and HslU (ClpY, ClpX) have also been demonstrated in to be present in the genome of trypanosomatid protozoa. They are expressed as precursors, with a propeptide that is removed to produce the active protease. The protease is probably located in the kinetoplast (mitochondrion). Phylogenetic analysis shows that HslV and HslU from trypanosomatids form a single clad with other eubacterial homologues [
].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
The Coat F proteins contribute to the Bacillales spore coat. They occur multiple times in the genomes in which they are found. Bacillus subtilis endospore protein coats protect them and may play a role in their germination [
]. Spore coat protein F, on the outer surface of the endospore, is one of a suite of proteins that could be used to differentiate between members of the Bacillus genus [].This group represents a spore coat protein F, CotF type.
The Coat F proteins contribute to the Bacillales spore coat. They occur multiple times in the genomes in which they are found. Bacillus subtilis endospore protein coats protect them and may play a role in their germination [
]. Spore coat protein F, on the outer surface of the endospore, is one of a suite of proteins that could be used to differentiate between members of the Bacillus genus [].
Members of the NSCC2 family have been sequenced from various fungal and animal species including Saccharomyces cerevisiae, Drosophila melanogaster and Homo sapiens. These proteins are the Sec62 proteins, believed to be associated with the Sec61 and Sec63 constituents of the general protein secretary systems of yeast microsomes. They are also the non-selective cation (NS) channels of the mammalian cytoplasmic membrane. The yeast Sec62 protein has been shown to be essential for cell growth. The mammalian NS channel proteins have been implicated in platelet derived growth factor(PGDF) dependent single channel current in fibroblasts. These channels are essentially closed in serum deprived tissue-culture cells and are specifically opened by exposure to PDGF. These channels are reported to exhibit equal selectivity for Na+, K+ and Cs+ with low permeability to Ca2+, and no permeability to anions.This family of Sec62 proteins is restricted to the Ascomycota.
This entry contains rotaviral non-structural protein 4 (NSP4) as well as related proteins: NSP5, NS28, and NCVP5. The final steps in the assembly of rotavirus occur in the lumen of the endoplasmic reticulum (ER). Targeting of the immature inner capsid particle (ICP) to this compartment is mediated by the cytoplasmic tail of NSP4, located in the ER membrane [
,
].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
Nuclear factor interleukin-3-regulated protein (NFIL3, also known as E4BP4) was first identified as a transcriptional repressor capable of binding an activating transcription factor (ATF) DNA consensus sequence site in the adenovirus E4 promoter [
]. Later, it was independently identified as a transactivator of the IL3 promoter in human T cells [].E4BP4 is involved in a several biological processes, including transcriptional control of the circadian clock, neuron growth and survival, osteoblast function, and regulation of ovulation [
]. It is essential for the development of NK cells and CD8alpha(+) conventional dendritic cells, and is also involved in macrophage activation, polarisation of CD4(+) T cell responses and B cell class switching to IgE [].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. They do show distant similarity to NTPases and to nucleic acid binding enzymes.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
This entry includes the cyanate transport protein CynX and 2-nitroimidazole transporter yeaN from E. coli.Protein yeaN is involved in efflux of 2-nitroimidazole [
]. Proteins expressed from the the cyn operon (indluding cynT, cynX, and cynS) in Escherichia coli are believed to transport cyanate into the cell so it can be metabolized into ammonia and bicarbonate [
]. This process is used to overcome the toxicity of environmental cyanate. CynT is a cyanate permease, CynS is a cyanase, while the function of the CynX is unknown [,
].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
This family contains uncharacterised proteins conserved in archaea. One family member (MJ1481) has been reported to be SepCysE, a translation factor, essential for the methanococcal Cys biosynthesis. SepCysE forms a bridge between Sep-tRNA:Cys-tRNA synthase (SepCysS) and O-phosphoseryl-tRNA synthetase (SepRS), forming the transsulfursome complex [
], enabling substrate channelling of Sep-tRNACys [].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
Shwachman-Bodian-Diamond syndrome (SDS) is an autosomal disorder with pancreatic, skeletal and bone marrow deficiencies and a predisposition to hematological dysfunction. The syndrome is associated with mutations in the SBDS gene, which encodes a protein that is required for biogenesis of the 60S ribosomal subunit and activation of the ribosome []. Maturation of the ribosomal 60S subunit requires SBDS and the GTPase EFL1, which release the anti-association factor eIF6 from the surface of the ribosomal subunit 60S []. In yeast, SBDS is known as Sdo1, which with the EF-2-like GTPase Ria1, may trigger the GTP-dependent release of Tif6 from 60S pre-ribosomes in the cytoplasm, thereby activating them [].
The proteins in this family are non-structural protein 1 (NSP1), also known as non-structural RNA-binding protein 53(NS53). They are RNA binding proteins that contain a characteristic cysteine rich region [
,
]. They are made at low levels in infected cells and are a component of early replication and are known to accumulate on the cytoskeleton of the infected cell.
Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [
,
]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [
,
].Ribosomal protein L1 is the largest protein from the large ribosomal subunit. In Escherichia coli, L1 is known to bind to the 23S rRNA. This model describes the mitochondrial L1 protein.
Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [
,
]. About2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.
Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [
,
].Ribosomal protein L1 is the largest protein from the large ribosomal subunit. The L1 protein contains two domains: 2-layer alpha/beta domain and a 3-layer alpha/beta domain (interrupts the first domain). In Escherichia coli, L1 is known to bind to the 23S rRNA. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [
,
], groups:Eubacterial L1Algal and plant chloroplast L1Cyanelle L1Archaebacterial L1Vertebrate L10AYeast SSM1This entry represents ribosomal L1P from the archaea; it binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and it is involved in E site tRNA release.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
Members of this uncharacterised protein family are found sporadically, so far only among spirochetes, epsilon and delta proteobacteria, and Bacteroides. The function is unknown and its gene neighbourhoods show little conservation.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
This entry specifically represents bacterial YdeI. YdeI is important for resistance to polymyxin B in broth and for bacterial survival in mice upon oral, but not intraperitoneal inoculation, suggesting a role for YdeI in the gastrointestinal tract of mice [
]. Production of the ydeI gene is regulated by the Rcs (regulator of capsule synthesis) phospho-relay system pathway independently of RcsA, and additionally transcription of the protein is regulated by the stationary-phase sigma factor, RpoS (sigma-S) []. YdeI confers protection against cationic AMPs (antimicrobial peptides) or bacteriocins in conjunction with the general porin Omp, thus justifying its name of OmdA, for OmpD-Associated protein [
].
This entry represents ComG operon protein 4 (also known as ComGD). The comG operon of Bacillus subtilis encodes seven membrane associated proteins, which function in binding of transforming DNA to the competent cell surface [
]. ComGC, GD, GE and GG have N-terminal sequence motifs typical of type 4 pre-pilins and are processed by a pathway that requires the product of comC, also an essential competence gene. They form form pilin-like structures that are localised to the cytoplasmic membrane and cell wall []. The comG operon also consist of ComGF, a small integral membrane protein, ComGA and ComGB, which are predicted to be a nucleotide binding protein and an integral membrane protein respectively []. When strains missing each of the 7 proteins are created, they were all found to be nontransformable and failed to bind transforming DNA to the cell surface [].
Cobalamin (Cbl or vitamin B12) is only accessible through diet in mammals. Absorption, plasma transport and cellular uptake of Cbl in mammals involves three Cbl-transporting proteins, which are listed below in order of increasing Cbl-specificity:Haptocorrin (cobalophilin), which binds Cbl and Cbl-derivatives such as cobinamide; it may play a role in preventing the absorption of cobalamin analogues produced by bacteria.Transcobalamin (TC), which transport Cbl from blood to cells.Intrinsic factor (IF), which promotes Cbl absorption in the ileum by specific receptor-mediated endocytosis.The structure of TC reveals a two-domain structure, an N-terminal alpha(6)-alpha(6) barrel, and a smaller C-terminal domain [
]. Many interactions between Cbl and its binding site in the interface of the two domains are conserved among the other Cbl transporters. Specificity for Cbl between the different transporters may reside in a β-hairpin motif found in the smaller C-terminal domain [].
This entry represents a group of heat shock proteins, including HSP21 from Arabidopsis. HSP21 interacts with plastid nucleoid protein pTAC5 and is essential for chloroplast development under heat stress by maintaining PEP (plastid-encoded RNA polymerase) function [
]. This family also includes small heat shock proteins from bacteria, such as HspC1/C3 from Rickettsia bellii.
E protein causes host cell lysis by inhibiting MraY, a peptidoglycan biosynthesis enzyme. This leads to cell wall failure at septation [
]. The N-terminal transmembrane region matches the signal peptide model and must be omitted from the family.
This is a bacterial family of proteins that are required for the formation of functionally normal spores. Proteins in this family may be involved in establishing normal coat structure and/or permeability which could control the access of germinants to their receptor [
].
Adenoviruses E4 is essential for DNA replication and late protein synthesis [
]. The adenovirus, early region 4 open reading frame 3 (E4 ORF3) protein is required for viral DNA replication during the interferon (IFN)-induced antiviral state [].The E4 ORF3 protein reorganises the promyelocytic leukemia (PML) protein nuclear bodies. These normally punctate structures are reorganised by E4 ORF3 into tracks that eventually surround viral replication centres. PML rearrangement is an evolutionarily conserved function of E4 ORF3 [
].The product of adenovirus early region 4 (E4), open reading frame 6, is E4 34k. It modulates viral late gene expression, DNA replication, apoptosis, double strand break repair, and transformation through multiple interactions with components in infected and transformed cells [
,
]. Conservation of several cysteine and histidine residues among E4 34k sequences suggests the presence of a zinc binding domain, which is important for its function [].
UL20 is predicted to be a transmembrane protein with multiple membrane spans. It is involved in the trans-cellular transport of enveloped virions, and is therefore important for viral egress. However, UL20 operates in different cellular compartments and different stages of egress in Suid herpesvirus 1 (Pseudorabies virus) and herpes simplex virus. This is thought to be due to differences in egress pathways between these two viruses [
].
This entry represents a group of plant WD repeat-containing proteins, including RUP1/2 (or EFO1/2) from Arabidopsis. EFO2 acts as a floral repressor, while EFO1 may not be directly involved in flowering, however, they have overlapping roles in regulating other developmental processes. Moreover, both EFO1/2 genes are regulated by the circadian clock [
].
Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport [
]. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis [].This entry also includes Alp41 from fission yeasts which is essential for the cofactor-dependent biogenesis of microtubules [].
This entry represents Ycf34, a protein encoded in algal genomes and additionally found in cyanobacteria. The function is not known. As the family is exclusively found in phototrophic organisms it may play a role in photosynthesis.
This entry represents the late protein H2 found in Vaccinia and other poxviruses. This protein is a highly conserved viral membrane protein found in all sequenced poxviruses, containing an N-terminal transmembrane domain and four conserved cysteines thought to be involved in the formation of intramolecular disulphide bonds [
]. H2 has been shown to be necessary for entry into the host cell and virus-induced cell-cell fusion, but is not required for virus morphogenesis or the attachment of virus particles to cells. It is part of an entry-fusion complex composed of eight viral membrane proteins [].
Pentatricopeptide repeat-containing protein At1g26460-like
Type:
Family
Description:
This entry represents a group of plant pentatricopeptide repeat-containing proteins, including At1g26460 from Arabidopsis. At1g26460 is a mitochondrial protein that binds RNA [
,
].
This domain of unknown function is found in the intermediate/early proteins of the Herpes virus. Many of these proteins play a role in transcriptional regulation.
This entry represents a group of plant RING-H2 finger proteins, including ATL10 and ATL75-79 from Arabidopsis. They are ubiquitin ligases that contain a RING-H2 domain [
].
This entry represents a group of plant RING-H2 finger proteins, including ATL1 and ATL16 from Arabidopsis. They are ubiquitin ligases that contain a RING-H2 domain [
,
]. ATL1 plays a central role in regulating plant defense responses and programmed cell death []. ATL16 is involved in carbon (C) and nitrogen nutrients (N) regulation and the defense response [].
This family of proteins regulates the replication of rolling circle replication (RCR) plasmids that have a double-strand replication origin (dso). Regulation of the replication of the RCR plasmids occurs mainly at the initiation of leading strand synthesis at the dso, such that concentration of Rep protein controls plasmid replication [
].
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
There is currently no experimental data for members of this group or their homologues, nor do they exhibit features indicative of any function. Members of this entry are mainly found in proteobacteria.
This is a family of keratins, high-sulphur matrix proteins. The keratin products of mammalian epidermal derivatives such as wool and hair consist of microfibrils embedded in a rigid matrix of other proteins. The matrix proteins include the high-sulphur and high-tyrosine keratins, having molecular weights of 6-20kDa, whereas microfibrils contain the larger, low-sulphur keratins (40-56kDa) [
].
In some species of plants the ycf15 gene is probably not a protein-coding gene because the protein in these species has premature stop codons. Most of the members of the family are hypothetical or uncharacterised [
].
The LanC-like protein superfamily encompasses a highly divergent group of peptide-modifying enzymes, including the eukaryotic and bacterial lanthionine synthetase C-like proteins (LanC) [
,
,
]; subtilin biosynthesis protein SpaC from Bacillus subtilis [,
]; epidermin biosynthesis protein EpiC from Staphylococcus epidermidis []; nisin biosynthesis protein NisC from Lactococcus lactis [,
,
]; GCR2 from Arabidopsis thaliana []; and many others. The 3D structure of the lantibiotic cyclase from L. lactis has been determined by X-ray crystallography to 2.5A resolution [
]. The globular structure is characterised by an all-α fold, in which an outer ring of helices envelops an inner toroid composed of 7 shorter, hydrophobic helices. This 7-fold hydrophobic periodicity has led several authors to claim various members of the family, including eukaryotic LanC-1 and GCR2, to be novel G protein-coupled receptors [,
]; some of these claims have since been corrected [,
,
]. The SpacC protein from B. subtilis is a cyclase enzyme involved in the biosynthesis of the lantibiotic subtilin [
,
,
].The protein exists as a monomer in solution and contains a stoichiometric zinc atom [], two cysteines and two histidines possibly acting as ligands to the metal; these cysteine residues are highly conserved in LanC-like proteins.
