id stringlengths 14 14 | text stringlengths 9 3.55k | source stringlengths 1 250 |
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c_uks4fp94piwj | Hbl, cytotoxin K (CytK) and Nhe are all putative causes. Both Hbl and Nhe are three-component cytotoxins composed of a binding component, B, and two lytic components, L1 and L2. All three subunits act synergically to cause hemolysis. | Bacillus haemolytic enterotoxin |
c_92qtlp7ezje4 | Maximal cytotoxicity of Nhe against epithelia is dependent on all three components. Nhe has haemolytic activity against erythrocytes from a variety of species. | Bacillus haemolytic enterotoxin |
c_67bodigznavl | It is possible that the common structural and functional properties of these toxins indicate that the Hbl/Nhe and ClyA families of toxins constitute a superfamily of pore-forming cytotoxins. Haemolysin BL and non-haemolytic enterotoxin production are both influenced by pH and micro. == References == | Bacillus haemolytic enterotoxin |
c_pbngb802xj6j | In molecular biology, the Bcl-x interacting domain is a protein domain found in BAM, Bim and Bcl2-like protein 11. It is a long alpha helix, which is required for interaction with Bcl-x. == References == | Bcl-x interacting domain |
c_58lnhk1vw9x6 | In molecular biology, the BmKK2 toxins are a family of scorpion toxins. They belong to the scorpion toxin subfamily alpha-KTx 14. They include a novel short-chain peptide from the Asian scorpion Mesobuthus martensii Karsch, a potassium channel blocker composed of 31 amino acid residues. The peptide adopts a classical a... | BmKK2 toxin |
c_af64nfk9t1b7 | BmKK2 selectively inhibits the delayed rectifier K+ current, but does not affect the fast transient K+ current.In comparison with typical short-chain scorpion toxins (e.g., CTX and NTX), the alpha helix is shorter and the beta-sheet element is smaller (each strand consists of only two residues). There is an alpha-mode ... | BmKK2 toxin |
c_riyij6ogoe1u | In molecular biology, the BolA-like protein family consists of the morpho-protein BolA from Escherichia coli, the Fra2 protein from Saccharomyces cerevisiae, and various homologs. The BolA protein is a DNA-binding regulator; the Fra2 protein is an iron sulfur cluster protein that binds Grx3/4 and is involved in regulat... | BolA-like protein family |
c_rthukvrb7phz | BolA is also induced by stress during early stages of growth and may have a general role in stress response. It has also been suggested that BolA can induce the transcription of penicillin binding proteins 6 and 5. == References == | BolA-like protein family |
c_qs05vmgxvfnu | In molecular biology, the Bowman–Birk protease inhibitor family of proteins consists of eukaryotic proteinase inhibitors, belonging to MEROPS inhibitor family I12, clan IF. They mainly inhibit serine peptidases of the S1 family, but also inhibit S3 peptidases.Members of this family have a duplicated structure and gener... | Bowman–Birk protease inhibitor |
c_083anq6kx464 | Proteins of the Bowman–Birk inhibitor family of serine proteinase inhibitors interact with the enzymes they inhibit via an exposed surface loop that adopts the canonical proteinase inhibitory conformation. The resulting noncovalent complex renders the proteinase inactive. This inhibition mechanism is common for the maj... | Bowman–Birk protease inhibitor |
c_rtt6rnn5am1z | In molecular biology, the BsuBI/PstI restriction endonuclease family is a family of type II restriction endonucleases. It includes BsuBI and PstI. The enzymes of the BsuBI restriction/modification (R/M) system recognise the target sequence 5'CTGCAG and are functionally identical with those of the PstI R/M system. == Re... | BsuBI/PstI restriction endonuclease |
c_am36ocaj79zm | In molecular biology, the Btk-type zinc finger or Btk motif (BM) is a conserved zinc-binding motif containing conserved cysteines and a histidine that is present in certain eukaryotic signalling proteins. The motif is named after Bruton's tyrosine kinase (Btk), an enzyme which is essential for B cell maturation in huma... | Btk-type zinc finger |
c_iyqfqo2e9p7d | The N-terminal of the TH domain is highly conserved and known as the Btf motif, while the C-terminal region of the TH domain contains a proline-rich region (PRR). The Btk motif contains a conserved His and three Cys residues that form a zinc finger (although these differ from known zinc finger topologies), while PRRs a... | Btk-type zinc finger |
c_z4xk8x7piq4l | A complete TH domain, containing both the Btk and PRR regions, has not been found outside the Tec family; however, the Btk motif on its own does occur in other proteins, usually C-terminal to a PH domain (note that although a Btk motif always occurs C-terminal to a PH domain, not all PH domains are followed by a Btk mo... | Btk-type zinc finger |
c_g47geptk1llc | Mutations affecting Btk are the cause of X-linked agammaglobulinemia (XLA) in humans and X-linked immunodeficiency in mice. Mammalian Tec, Bmx, and Itk proteins, which are tyrosine protein kinases of the Tec subfamily. | Btk-type zinc finger |
c_8av5djw1xk51 | Drosophila tyrosine-protein kinase Btk29A, which is required for the development of proper ring canals and of male genitalia and required for adult survival. Mammalian Ras GTPase-activating proteins (RasGAP), which regulate the activation of inactive GDP-bound Ras by converting GDP to GTP. == References == | Btk-type zinc finger |
c_27391yprwj0j | In molecular biology, the BtpA protein family is a family of proteins which includes BtpA. BtpA appears to play a role in the stabilisation of photosystem I . It is an extrinsic membrane protein located on the cytoplasmic side of the thylakoid membrane. Homologs of BtpA are found in the Thermoproteota and "Euryarchaeot... | BtpA protein |
c_930etmsex6r8 | The Ycf4 protein is firmly associated with the thylakoid membrane, presumably through a transmembrane domain. Ycf4 co-fractionates with a protein complex larger than PSI upon sucrose density gradient centrifugation of solubilised thylakoids. The Ycf3 protein is loosely associated with the thylakoid membrane and can be ... | BtpA protein |
c_nmm0jeojamwf | This suggests that Ycf3 is not part of a stable complex and that it probably interacts transiently with its partners. Ycf3 contains a number of tetratricopeptide repeats (TPR); TPR is a structural motif present in a wide range of proteins, which mediates protein-protein interactions. == References == | BtpA protein |
c_jbiwfwg1t0mz | In molecular biology, the Btz domain (CASC3/Barentsz eIF4AIII binding domain) is a protein domain found on CASC3 (cancer susceptibility candidate gene 3 protein) which is also known as Barentsz (Btz). CASC3 is a component of the EJC (exon junction complex) which is a complex that is involved in post-transcriptional reg... | Btz domain |
c_j7i9fpomtowx | In molecular biology, the CAS/CSE protein family is a family of proteins which includes mammalian cellular apoptosis susceptibility (CAS) proteins and yeast chromosome-segregation protein, CSE1. CAS is involved in both cellular apoptosis and proliferation. Apoptosis is inhibited in CAS-depleted cells, while the express... | CAS/CSE protein family |
c_8jclip9rcxx8 | In the nucleus, CAS acts as a nuclear transport factor in the importin pathway. The importin pathway mediates the nuclear transport of several proteins that are necessary for mitosis and further progression. CAS is therefore thought to affect the cell cycle through its effect on the nuclear transport of these proteins. | CAS/CSE protein family |
c_ase5o06nnhxb | Since apoptosis also requires the nuclear import of several proteins (such as P53 and transcription factors), it has been suggested that CAS also enables apoptosis by facilitating the nuclear import of at least a subset of these essential proteins.Members of the CAS/CSE family of proteins have two domains. An N-termina... | CAS/CSE protein family |
c_rtatgdgqjjsc | In molecular biology, the CAT RNA-binding domain (Co-AntiTerminator RNA-binding domain) is a protein domain found at the amino terminus of a family of transcriptional antiterminator proteins. This domain forms a dimer in the crystal structure. Transcriptional antiterminators of the BglG/SacY family are regulatory prote... | CAT RNA-binding domain |
c_e89tjy2jsr4l | In molecular biology, the CBS domain is a protein domain found in a range of proteins in all species from bacteria to humans. It was first identified as a conserved sequence region in 1997 and named after cystathionine beta synthase, one of the proteins it is found in. CBS domains are also found in a wide variety of ot... | CBS domain |
c_1euoe6kj8zlq | In molecular biology, the CD20-like family of proteins includes the CD20 protein and the beta subunit of the high affinity receptor for IgE Fc, MS4A2. MS4A2 has a tetrameric structure consisting of a single IgE-binding alpha subunit, a single beta subunit, and two disulfide-linked gamma subunits. It has four putative t... | CD20-like family |
c_zcqtmu167j3g | This family also includes LR8 like proteins from humans (TMEM176B), mice and rats. The function of the human LR8 protein is unknown although it is known to be strongly expressed in the lung fibroblasts. This family also includes sarcospan, a transmembrane component of dystrophin-associated glycoprotein. | CD20-like family |
c_ly11nx0uasiv | Loss of the sarcoglycan complex and sarcospan alone is sufficient to cause muscular dystrophy. The role of the sarcoglycan complex and sarcospan is thought to be to strengthen the dystrophin axis connecting the basement membrane with the cytoskeleton. == References == | CD20-like family |
c_0ccz9ynlev8x | In molecular biology, the CDC48 N-terminal domain is a protein domain found in AAA ATPases including cell division protein 48 (CDC48), VCP-like ATPase and N-ethylmaleimide sensitive fusion protein. It is a substrate recognition domain which binds polypeptides, prevents protein aggregation, and catalyses refolding of pe... | CDC48 N-terminal domain |
c_l88ujq1npudq | The carboxy-terminal subdomain (CDC48_2) forms a novel six-stranded beta-clam fold. Together these subdomains form a kidney-shaped structure, in close agreement with results from electron microscopy. CDC48_N is related to numerous proteins including prokaryotic transcription factors, metabolic enzymes, the protease cof... | CDC48 N-terminal domain |
c_fcicz89w7jko | In molecular biology, the CFC domain (Cripto_Frl-1_Cryptic domain) is a protein domain found at the C-terminus of a number of proteins including Cripto (or teratocarcinoma-derived growth factor). It is structurally similar to the C-terminal extracellular portions of Jagged 1 and Jagged 2. CFC is approx 40-residues long... | CFC domain |
c_vo7lyg9jc1ql | In molecular biology, the CHAP domain is a region between 110 and 140 amino acids that is found in proteins from bacteria, bacteriophages, archaea and eukaryotes of the family Trypanosomidae. The domain is named after the acronym cysteine, histidine-dependent amidohydrolases/peptidases. Many of these proteins are uncha... | CHAP domain |
c_6tu4creymuwp | It has been suggested that CHAP domain containing proteins utilise a catalytic cysteine residue in a nucleophilic-attack mechanism.The CHAP domain contains two invariant residues, a cysteine and a histidine. These residues form part of the putative active site of CHAP domain containing proteins. Secondary structure pre... | CHAP domain |
c_a3vz6s3j055w | A variety of bacterial autolysins. A Nocardia aerocolonigenes putative esterase. Streptococcus pneumoniae choline-binding protein D. Methanosarcina mazei protein MM2478, a putative chloride channel. | CHAP domain |
c_3zw9tdu5vydk | Several phage-encoded peptidoglycan hydrolases. Cysteine peptidases belonging to MEROPS peptidase family C51 (D-alanyl-glycyl endopeptidase, clan CA). == References == | CHAP domain |
c_ofyky0mk84jh | In molecular biology, the CHB HEX N-terminal domain represents the N-terminal domain in chitobiases and beta-hexosaminidases. Chitobiases degrade chitin, which forms the exoskeleton in insects and crustaceans, and which is one of the most abundant polysaccharides on earth. Beta-hexosaminidases are composed of either a ... | CHB HEX N-terminal domain |
c_flots291qlwy | HexB is structurally similar to chitobiase, consisting of a beta sandwich structure; this structure is similar to that found in the cellulose-binding domain of cellulase from Cellulomonas fimi. This domain may function as a carbohydrate binding module. == References == | CHB HEX N-terminal domain |
c_xvofz1z0xl44 | In molecular biology, the CLP protease family is a family of serine peptidases belong to the MEROPS peptidase family S14 (ClpP endopeptidase family, clan SK). ClpP is an ATP-dependent protease that cleaves a number of proteins, such as casein and albumin. It exists as a heterodimer of ATP-binding regulatory A and catal... | CLP protease family |
c_xusbe90zt66j | In molecular biology, the CRM domain is an approximately 100-amino acid RNA-binding domain. The name CRM (chloroplast RNA splicing and ribosome maturation) has been suggested to reflect the functions established for four characterised members of the family: Zea mays (Maize) CRS1, CAF1 and CAF2 proteins and the Escheric... | CRM domain |
c_vxz4dnq6qo5c | It has been suggested that prokaryotic CRM proteins existed as ribosome-associated proteins prior to the divergence of archaea and bacteria, and that they were co-opted in the plant lineage as RNA binding modules by incorporation into diverse protein contexts. Plant CRM domains are predicted to reside not only in the c... | CRM domain |
c_hgzwh65uek7v | The beta sheet face is basic, consistent with a role in RNA binding. Proximal to the basic beta sheet face is another moiety that could contribute to nucleic acid recognition. Connecting strand beta1 and helix alpha2 is a loop with a six amino acid motif, GxxG flanked by large aliphatic residues, within which one 'x' i... | CRM domain |
c_lagktrr9axyh | GFP fused to a single-domain CRM protein from maize localises to the nucleolus, suggesting that an analogous activity may have been retained in plants. A CRM domain containing protein in plant chloroplasts has been shown to function in group I and II intron splicing. In vitro experiments with an isolated maize CRM doma... | CRM domain |
c_fuzujabqbn7l | These and other results suggest that the CRM domain evolved in the context of ribosome function prior to the divergence of Archaea and Bacteria, that this function has been maintained in extant prokaryotes, and that the domain was recruited to serve as an RNA binding module during the evolution of plant genomes. YhbY h... | CRM domain |
c_jrbrkzljo6rn | In molecular biology, the CRP domain is a protein domain consisting of a helix-turn-helix (HTH) motif. It is found at the C-terminus of numerous bacterial transcription regulatory proteins. These proteins bind DNA via the CRP domain. | Crp domain |
c_w2yvvy9mew22 | These proteins are very diverse, but for convenience may be grouped into subfamilies on the basis of sequence similarity. This family groups together a range of proteins, including ANR, CRP, CLP, CysR, FixK, Flp, FNR, FnrN, HlyX and NtcA. == References == | Crp domain |
c_2ncrbp6orns1 | In molecular biology, the CUT domain (also known as ONECUT) is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, which is often found downstream of the CUT domain. Proteins display two modes of DNA binding, which hinge on the homeodomain and on the linker that separates it from th... | CUT domain |
c_gtge4ko9pi42 | In molecular biology, the CVNH domain (CyanoVirin-N Homology domain) is a conserved protein domain. It is found in the sugar-binding antiviral protein cyanovirin-N (CVN) as well as proteins from filamentous ascomycetes and in the fern Ceratopteris richardii.Cyanovirin-N (CV-N) is an 11-kDa protein from the cyanobacteri... | CVNH domain |
c_4m6lxymb78rh | The virucidal activity of CV-N against influenza virus is directed towards viral haemagglutinin. CV-N has a complex fold composed of a duplication of a tandem repeat of two homologous motifs comprising three-stranded beta sheet and beta hairpins. == References == | CVNH domain |
c_v17nigtv6ll0 | In molecular biology, the Cbl TKB domain (tyrosine kinase binding domain), also known as the phosphotyrosine binding (PTB) domain is a conserved region found at the N-terminus of Cbl adaptor proteins. This N-terminal region is composed of three evolutionarily conserved domains: an N-terminal four-helix bundle domain, a... | Cbl TKB domain |
c_l120qwlvrd0a | In molecular biology, the Cfr10I/Bse634I family of restriction endonucleases includes the type II restriction endonucleases Cfr10I and Bse634I. They exhibit a conserved tetrameric architecture that is of functional importance, wherein two dimers are arranged, back-to-back, with their putative DNA-binding clefts facing ... | Cfr10I/Bse634I |
c_01bymoj32j3y | Each monomer is folded to form a compact alpha-beta structure, whose core is made up of a five-stranded mixed beta-sheet. The monomer may be split into separate N-terminal and C-terminal subdomains at a hinge located in helix alpha3. Both Cfr10I and Bse634I recognise the double-stranded sequence RCCGGY and cleave after... | Cfr10I/Bse634I |
c_cnx3vgeed2vs | In molecular biology, the CodY protein family consists of several bacterial GTP-sensing transcriptional pleiotropic repressor CodY proteins. CodY has been found to repress the dipeptide transport operon (dpp) of Bacillus subtilis in nutrient-rich conditions. The CodY protein also has a repressor effect on many genes in... | CodY protein family |
c_qarr93r2s3pk | In molecular biology, the Cofactor transferase family is a family of protein domains that includes biotin protein ligases, lipoate-protein ligases A, octanoyl-(acyl carrier protein):protein N-octanoyltransferases, and lipoyl-protein:protein N-lipoyltransferases. The metabolism of the cofactors Biotin and lipoic acid sh... | Cofactor transferase family |
c_1sqjjeaa8itm | Each organism likely has only one BPL protein. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Biotin attachment is required for biotin biosynthesis and utilization of free biotin.Lipoate-... | Cofactor transferase family |
c_r3tfdpm0j8ph | They are required for the utilization of free lipoic acid.Octanoyl-(acyl carrier protein):protein N-octanoyltransferases, or octanoyltransferases, are required for lipoic acid biosynthesis. They transfer octanoate from the acyl carrier protein (ACP), part of fatty acid biosynthesis, to the specific lysine residue of li... | Cofactor transferase family |
c_g6rav2kyqeb9 | They transfer lipoic acid or octanoate from lipoyl domains and transfer to other lipoyl domains. In Bacillus subtilis, the transfer is from the glycine cleavage system H protein, GcvH, to other lipoyl domains. This is because the octanoyltransferase of B. subtilis is specific for GcvH. | Cofactor transferase family |
c_ix5djaf6dwpu | In molecular biology, the Cro repressor family is a family of repressor proteins in bacteriophage lambda that includes the Cro repressor. Bacteriophage lambda encodes two repressors: the Cro repressor that acts to turn off early gene transcription during the lytic cycle, and the lambda or cI repressor required to maint... | Cro repressor family |
c_b93xk6inlcn2 | The crystal structure of the lambda Cro repressor reveals a HTH DNA-binding protein with an alpha/beta fold that differs from other Cro family members, possibly by an evolutionary fold change. Most Cro proteins, such as Enterobacteria phage P22 Cro and Bacteriophage 434 Cro, have an all-alpha structure that is thought ... | Cro repressor family |
c_c884zipa8q81 | In molecular biology, the Cys/Met metabolism PLP-dependent enzyme family is a family of proteins including enzymes involved in cysteine and methionine metabolism which use PLP (pyridoxal-5'-phosphate) as a cofactor. | Cys/Met metabolism PLP-dependent enzyme family |
c_fcuqtxq3sd4l | In molecular biology, the DEP domain (Dishevelled, Egl-10 and Pleckstrin domain) is a globular protein domain of about 80 amino acids that is found in over 50 proteins involved in G-protein signalling pathways. It was named after the three proteins it was initially found in: Dishevelled (Dsh and Dvl), which plays a key... | DEP domain |
c_rmx4p9bdsbaa | It has been proposed that the DEP domain could play a selective role in targeting DEP domain-containing proteins to specific subcellular membranous sites, perhaps even to specific G protein-coupled signaling pathways. Nuclear magnetic resonance spectroscopy has revealed that the DEP domain comprises a three-helix bundl... | DEP domain |
c_r5p9a6yg6dlv | In molecular biology, the DHH phosphatase family is a family of putative phosphoesterases. The family includes Drosophila prune protein and bacterial RecJ exonuclease. The RecJ protein of Escherichia coli plays an important role in a number of DNA repair and recombination pathways. | DHH phosphatase family |
c_awynagirpkr5 | RecJ catalyses processive degradation of single-stranded DNA in a 5'-to-3' direction. Sequences highly related to those encoding RecJ can be found in many of the eubacterial genomes sequenced to date. == References == | DHH phosphatase family |
c_vnbzowzvu2xp | In molecular biology, the DSS1/SEM1 protein family is a family of short acidic proteins which includes the 26S proteasome complex subunits SEM1 from Saccharomyces cerevisiae and Drosophila and DSS1 (SHFM1) in mammals. In Saccharomyces cerevisiae, SEM1 is a regulator of both exocyst function and pseudohyphal differentia... | DSS1/SEM1 protein family |
c_047jf7r9fbb6 | In molecular biology, the DinI-like protein family is a family of short proteins. The family includes DNA-damage-inducible protein I (DinI) and related proteins. The SOS response, a set of cellular phenomena exhibited by eubacteria, is initiated by various causes that include DNA damage-induced replication arrest, and ... | DinI-like protein family |
c_ol6g4hwg0lz5 | Biochemical and genetic studies indicated that DinI physically interacts with RecA to inhibit its co-protease activity. The structure of DinI is known. == References == | DinI-like protein family |
c_yzmvwj9ngvwb | In molecular biology, the DmpG-like communication domain is a protein domain found towards the C-terminal region of various aldolase enzymes. It consists of five alpha-helices, four of which form an antiparallel helical bundle that plugs the C terminus of the N-terminal TIM barrel domain. The communication domain is th... | DmpG-like communication domain |
c_7m9wjmnsgmai | In molecular biology, the DpnII restriction endonuclease family is a family of restriction endonucleases which includes DpnII from Diplococcus pneumoniae. These enzymes recognise the double-stranded DNA unmethylated sequence GATC and cleave before G-1, where it encompasses the full length of the protein. == References ... | DpnII restriction endonuclease family |
c_ytz3wy1xb0f9 | In molecular biology, the DyP-type peroxidase family is a family of haem peroxidase enzymes. Haem peroxidases were originally divided into two superfamilies, namely, the animal peroxidases and the plant peroxidases (which are subdivided into class I, II and III), which include fungal (class II) and bacterial peroxidase... | DyP-type peroxidase family |
c_yf3vgm5a11l8 | However, the DyP family exhibits only low sequence similarity to classical fungal peroxidases, such as LiP and MnP, and does not contain the conserved proximal and distal histidines and an essential arginine found in other plant peroxidase superfamily members. DyP proteins have several characteristics that distinguish ... | DyP-type peroxidase family |
c_a8souydcx2zz | Crystal structures of DyP family members reveal two domains, each one adopting a ferredoxin-like fold. The proteins consist of an N-terminal domain and a C-terminal domain likely to be related by a duplication of an ancestral gene, as inferred from the conserved topology of the domains. The haem iron is penta-coordinat... | DyP-type peroxidase family |
c_xvvjh7mn3l8p | A conserved Asp most likely acts as a proton donor/acceptor and takes the place of the catalytic histidine used by plant peroxidases. This Asp substitution helps explain why the DyP family is active at low pH. == References == | DyP-type peroxidase family |
c_zp6l2o13hn36 | In molecular biology, the Dymeclin protein family is a family of proteins which includes human Dymeclin. Dymeclin (Dyggve-Melchior-Clausen syndrome protein) contains a large number of leucine and isoleucine residues and a total of 17 repeated dileucine motifs. It is characteristically about 700 amino acids long and pre... | Dymeclin protein family |
c_2jsnrlk3ou1k | It contains up to seven potential transmembrane domains separated by regions of low complexity. Functionally this protein might be involved in vesicle secretion or be an inter-cellular signalling protein or be a novel insulin receptor. == References == | Dymeclin protein family |
c_ts0kb0fczf5q | In molecular biology, the EAL domain is a conserved protein domain. It is found in diverse bacterial signalling proteins. It is named EAL after its conserved residues. | EAL domain |
c_k2qcodpok44p | The EAL domain may function as a diguanylate phosphodiesterase. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site. == References == | EAL domain |
c_m6ik3uara7v1 | In molecular biology, the EF1 guanine nucleotide exchange domain is a protein domain found in the beta and delta chains of elongation factors from eukaryotes and archaea. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its ina... | EF1 guanine nucleotide exchange domain |
c_kehsw3fj22it | The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma). == References == | EF1 guanine nucleotide exchange domain |
c_lq8hii2hhv5k | In molecular biology, the ELFV dehydrogenase family of enzymes include glutamate, leucine, phenylalanine and valine dehydrogenases. These enzymes are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each cas... | ELFV dehydrogenase |
c_d72gfgd2b9mk | GluDH isozymes are generally involved with either ammonia assimilation or glutamate catabolism. Two separate enzymes are present in yeasts: the NADP-dependent enzyme, which catalyses the amination of alpha-ketoglutarate to L-glutamate; and the NAD-dependent enzyme, which catalyses the reverse reaction - this form links... | ELFV dehydrogenase |
c_ysg8ygh799ut | The nicotinamide ring of the NAD+ cofactor binds deep in this cleft, which is thought to close during the hydride transfer step of the catalytic cycle. Phenylalanine dehydrogenase EC 1.4.1.20 (PheDH) is an NAD-dependent enzyme that catalyses the reversible deamidation of L-phenylalanine into phenyl-pyruvate.Valine dehy... | ELFV dehydrogenase |
c_d37awqh4ju5g | In molecular biology, the EMI domain, first named after its presence in proteins of the EMILIN family, is a small cysteine-rich protein domain of around 75 amino acids. The EMI domain is most often found at the N terminus of metazoan extracellular proteins that are forming or are compatible with multimer formation. It ... | EMI domain |
c_1mw6n2ehj6yh | Other key features of the EMI domain are the C-C-x-G- pattern, a hydrophobic position just preceding the first cysteine (Cys1) of the domain and a cluster of hydrophobic residues between Cys3 and Cys4. The EMI domain could be made of two sub-domains, the fold of the second one sharing similarities with the C-terminal s... | EMI domain |
c_n02ng0q8w5df | Vertebrate Emu proteins, which could interact with several different extracellular matrix components and serve to connect and integrate the function of multiple partner molecules. Vertebrate beta-IG-H3. Vertebrate osteoblast-specific factor 2 (OSF-2). | EMI domain |
c_14cbpi0in6ar | Mammalian NEU1/NG3 proteins. Drosophila midline fasciclin. Caenorhabditis elegans ced-1, a transmembrane receptor that mediates cell corpse engulfment. == References == | EMI domain |
c_nyujvrb8het4 | In molecular biology, the EcoEI R protein C-terminal domain is a protein domain found at the C-terminus of both the R subunit of type I restriction enzymes and the Res subunit of type III restriction enzymes. The type I enzymes include EcoEI, which recognises 5'-GAGN(7)ATGC-3; the R protein (HsdR) is required for both ... | EcoEI R protein C-terminal domain |
c_648vxa8ixtta | In molecular biology, the F-actin capping protein is a protein complex which binds in a calcium-independent manner to the fast-growing ends of actin filaments (barbed end), thereby blocking the exchange of subunits at these ends. Unlike gelsolin and severin this protein does not sever actin filaments. The F-actin cappi... | F-actin capping protein |
c_rsk3kuopiy5m | Neither of the subunits shows sequence similarity to other filament-capping proteins. The alpha subunit is a protein of about 268 to 286 amino acid residues and the beta subunit is approximately 280 amino acids, their sequences are well conserved in eukaryotic species.The actin filament system, a prominent part of the ... | F-actin capping protein |
c_q1ews8p9p4an | In molecular biology, the FAD dependent oxidoreductase family of proteins is a family of FAD dependent oxidoreductases. Members of this family include Glycerol-3-phosphate dehydrogenase EC 1.1.99.5, Sarcosine oxidase beta subunit EC 1.5.3.1, D-amino-acid dehydrogenase EC 1.4.99.1, D-aspartate oxidase EC 1.4.3.1. D-amin... | FAD dependent oxidoreductase family |
c_o85hjybcwlzp | DAOs have been characterised and sequenced in fungi and vertebrates where they are known to be located in the peroxisomes. D-aspartate oxidase EC 1.4.3.1 (DASOX) is an enzyme, structurally related to DAO, which catalyses the same reaction but is active only toward dicarboxylic D-amino acids. In DAO, a conserved histidi... | FAD dependent oxidoreductase family |
c_54dgxsqa4n9r | In molecular biology, the FERM domain (F for 4.1 protein, E for ezrin, R for radixin and M for moesin) is a widespread protein module involved in localising proteins to the plasma membrane. FERM domains are found in a number of cytoskeletal-associated proteins that associate with various proteins at the interface betwe... | FERM domain |
c_oicvxysu1spa | In molecular biology, the FEZ-like protein family is a family of eukaryotic proteins thought to be involved in axonal outgrowth and fasciculation. The N-terminal regions of these sequences are less conserved than the C-terminal regions, and are highly acidic. The Caenorhabditis elegans homologue, UNC-76, may play struc... | FEZ-like protein |
c_p9ua8f92721f | The C-terminal region probably participates in the association with the regulatory domain of PKC-zeta. The members of this family are predicted to form coiled-coil structures which may interact with members of the RhoA family of signalling proteins, but are not thought to contain other characteristic protein motifs. Ce... | FEZ-like protein |
c_a9bgopvh45ry | In molecular biology, the FHIPEP protein family (Flagellar/Hr/Invasion Proteins Export Pore family)consists of a number of proteins that constitute the type III secretion (or signal peptide-independent) pathway apparatus. This mechanism translocates proteins lacking an N-terminal signal peptide across the cell membrane... | FHIPEP protein family |
c_z69fx6xfx6fi | An FHIPEP protein is located within the inner membrane, although it is unknown which component it constitutes. FHIPEP proteins have all about 700 amino acid residues. | FHIPEP protein family |
c_e4fh3txhr1p1 | Within the sequence, the N terminus is highly conserved and hydrophobic, suggesting that this terminus is embedded within the membrane, with 6-8 transmembrane (TM) domains, while the C terminus is less conserved and appears to be devoid of TM regions. It is possible that members of the FHIPEP family serve as pores for ... | FHIPEP protein family |
c_ym3l7ohqmvrq | In molecular biology, the FLYWCH zinc finger is a zinc finger domain. It is found in a number of eukaryotic proteins. FLYWCH is a C2H2-type zinc finger characterised by five conserved hydrophobic residues, containing the conserved sequence motif: F/Y-X(n)-L-X(n)-F/Y-X(n)-WXCX(6-12)CX(17-22)HXH where X indicates any ami... | FLYWCH zinc finger |
c_sl5vc058iii4 | This domain was first characterised in Drosophila modifier of mdg4 proteins, Mod(mgd4), putative chromatin modulators involved in higher order chromatin domains. Mod(mdg4) proteins share a common N-terminal BTB/POZ domain, but differ in their C-terminal region, most containing C-terminal FLYWCH zinc finger motifs. The ... | FLYWCH zinc finger |
c_jzjrk5awugb2 | In molecular biology, the Fic/DOC protein family is a family of proteins which catalyzes the post-translational modification of proteins using phosphate-containing compound as a substrate. Fic domain proteins typically use ATP as a co-factor, but in some cases GTP or UTP is used. Post-translational modification perform... | Fic/DOC protein family |
c_nxp8d3in50ns | In molecular biology, the GA module, or protein G-related albumin-binding module, is a protein domain which occurs on the surface of numerous Gram-positive bacterial pathogens. Protein G of group C and G Streptococci interacts with the constant region of IgG and with human serum albumin. The GA module is composed of a ... | GA module |
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