ComEC family DNA internalization-related competence protein similar to Bacillus subtilis ComE operon protein 3, which is required for DNA internalization; the comE operon is required for the binding and uptake of transforming DNA
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
65-718
0e+00
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]
Pssm-ID: 273036 [Multi-domain] Cd Length: 662 Bit Score: 1006.35 E-value: 0e+00
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
499-732
3.26e-77
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441904 [Multi-domain] Cd Length: 253 Bit Score: 249.00 E-value: 3.26e-77
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
500-664
1.95e-58
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293817 [Multi-domain] Cd Length: 179 Bit Score: 196.20 E-value: 1.95e-58
Competence protein; Members of this family are integral membrane proteins with 6 predicted ...
203-491
2.03e-47
Competence protein; Members of this family are integral membrane proteins with 6 predicted transmembrane helices. Some members of this family have been shown to be essential for bacterial competence in uptake of extracellular DNA. These proteins may transport DNA across the cell membrane. These proteins contain a highly conserved motif in the amino terminal transmembrane region that has two histidines that may form a metal binding site.
Pssm-ID: 461044 [Multi-domain] Cd Length: 269 Bit Score: 169.32 E-value: 2.03e-47
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
511-657
8.57e-10
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 58.72 E-value: 8.57e-10
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
65-718
0e+00
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]
Pssm-ID: 273036 [Multi-domain] Cd Length: 662 Bit Score: 1006.35 E-value: 0e+00
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
499-732
3.26e-77
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 441904 [Multi-domain] Cd Length: 253 Bit Score: 249.00 E-value: 3.26e-77
ComEC/Rec2-related protein; The related model ComEC_Rec2 (TIGR00361) describes a set of ...
221-405
2.01e-59
ComEC/Rec2-related protein; The related model ComEC_Rec2 (TIGR00361) describes a set of proteins of ~ 700-800 residues, one each from a number of different species, of which most can become competent for natural transformation with exogenous DNA. The best-studied examples are ComEC from Bacillus subtilis and Rec-2 from Haemophilus influenzae, where the protein appears to form part of the DNA import structure. This model represents a region found in full-length ComEC/Rec2 and shorter homologs of unknown function from large number of additional bacterial species, most of which are not known to become competent for transformation (an exception is Helicobacter pylori). [Unknown function, General]
Pssm-ID: 273035 [Multi-domain] Cd Length: 171 Bit Score: 198.37 E-value: 2.01e-59
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
500-664
1.95e-58
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293817 [Multi-domain] Cd Length: 179 Bit Score: 196.20 E-value: 1.95e-58
Competence protein; Members of this family are integral membrane proteins with 6 predicted ...
203-491
2.03e-47
Competence protein; Members of this family are integral membrane proteins with 6 predicted transmembrane helices. Some members of this family have been shown to be essential for bacterial competence in uptake of extracellular DNA. These proteins may transport DNA across the cell membrane. These proteins contain a highly conserved motif in the amino terminal transmembrane region that has two histidines that may form a metal binding site.
Pssm-ID: 461044 [Multi-domain] Cd Length: 269 Bit Score: 169.32 E-value: 2.03e-47
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
511-657
8.57e-10
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.
Pssm-ID: 214854 [Multi-domain] Cd Length: 177 Bit Score: 58.72 E-value: 8.57e-10
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293799 Cd Length: 269 Bit Score: 44.54 E-value: 1.10e-04
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
513-570
2.97e-04
mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.
Pssm-ID: 293792 [Multi-domain] Cd Length: 188 Bit Score: 42.66 E-value: 2.97e-04
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
500-573
3.58e-03
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.
Pssm-ID: 293807 [Multi-domain] Cd Length: 202 Bit Score: 39.51 E-value: 3.58e-03
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
512-578
4.17e-03
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.
Pssm-ID: 293800 [Multi-domain] Cd Length: 248 Bit Score: 39.70 E-value: 4.17e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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