RNase J family beta-CASP ribonuclease [Propionibacterium sp. HMSC062D05]
Protein Classification
ribonuclease J( domain architecture ID 11426779)
ribonuclease J 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
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| RnjA | COG0595 | mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; |
6-557 | 0e+00 | ||||||||
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; : Pssm-ID: 440360 [Multi-domain] Cd Length: 553 Bit Score: 834.33 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| RnjA | COG0595 | mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; |
6-557 | 0e+00 | ||||||||
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440360 [Multi-domain] Cd Length: 553 Bit Score: 834.33 E-value: 0e+00
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| MG423 | TIGR00649 | beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ... |
11-429 | 2.97e-149 | ||||||||
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA] Pssm-ID: 273195 [Multi-domain] Cd Length: 422 Bit Score: 435.24 E-value: 2.97e-149
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| RNaseJ_MBL-fold | cd07714 | RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ... |
14-429 | 3.24e-96 | ||||||||
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: 292.77 E-value: 3.24e-96
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| RNase_J_C | pfam17770 | Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ... |
460-557 | 2.38e-20 | ||||||||
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J proteins. Its function is unknown, but deletion of this domain causes dissociation to monomers. Pssm-ID: 436030 Cd Length: 102 Bit Score: 86.01 E-value: 2.38e-20
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| Lactamase_B | smart00849 | Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
27-219 | 2.29e-18 | ||||||||
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: 82.99 E-value: 2.29e-18
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| PRK11921 | PRK11921 | anaerobic nitric oxide reductase flavorubredoxin; |
62-142 | 1.96e-07 | ||||||||
anaerobic nitric oxide reductase flavorubredoxin; Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 53.54 E-value: 1.96e-07
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| Name | Accession | Description | Interval | E-value | ||||||||
| RnjA | COG0595 | mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; |
6-557 | 0e+00 | ||||||||
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440360 [Multi-domain] Cd Length: 553 Bit Score: 834.33 E-value: 0e+00
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| MG423 | TIGR00649 | beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ... |
11-429 | 2.97e-149 | ||||||||
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA] Pssm-ID: 273195 [Multi-domain] Cd Length: 422 Bit Score: 435.24 E-value: 2.97e-149
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| RNaseJ_MBL-fold | cd07714 | RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ... |
14-429 | 3.24e-96 | ||||||||
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: 292.77 E-value: 3.24e-96
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| metallo-hydrolase-like_MBL-fold | cd07732 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
12-171 | 1.59e-21 | ||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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, 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: 293818 [Multi-domain] Cd Length: 202 Bit Score: 92.68 E-value: 1.59e-21
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| YSH1 | COG1236 | RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ... |
12-247 | 1.76e-20 | ||||||||
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440849 [Multi-domain] Cd Length: 404 Bit Score: 93.71 E-value: 1.76e-20
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| RNase_J_C | pfam17770 | Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J ... |
460-557 | 2.38e-20 | ||||||||
Ribonuclease J C-terminal domain; This domain is found at the C-terminus of Ribonuclease J proteins. Its function is unknown, but deletion of this domain causes dissociation to monomers. Pssm-ID: 436030 Cd Length: 102 Bit Score: 86.01 E-value: 2.38e-20
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| ElaC | COG1234 | Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; |
11-205 | 3.78e-20 | ||||||||
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440847 [Multi-domain] Cd Length: 250 Bit Score: 89.87 E-value: 3.78e-20
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| TTHA0252-CPSF-like_MBL-fold | cd16295 | Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ... |
13-176 | 4.39e-19 | ||||||||
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain] Cd Length: 197 Bit Score: 85.59 E-value: 4.39e-19
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| Lactamase_B | smart00849 | Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
27-219 | 2.29e-18 | ||||||||
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: 82.99 E-value: 2.29e-18
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| PhnP | COG1235 | Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ... |
23-202 | 4.67e-15 | ||||||||
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; Pssm-ID: 440848 [Multi-domain] Cd Length: 259 Bit Score: 75.32 E-value: 4.67e-15
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| metallo-hydrolase-like_MBL-fold | cd06262 | mainly hydrolytic enzymes and related proteins which carry out various biological functions; ... |
28-169 | 8.05e-14 | ||||||||
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: 70.01 E-value: 8.05e-14
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| CPSF3-like_MBL-fold | cd16292 | cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ... |
11-92 | 1.01e-11 | ||||||||
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850 Cd Length: 194 Bit Score: 64.14 E-value: 1.01e-11
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| RNaseZ_short-form-like_MBL-fold | cd07716 | uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ... |
27-201 | 1.69e-11 | ||||||||
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial 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: 293802 [Multi-domain] Cd Length: 175 Bit Score: 62.84 E-value: 1.69e-11
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| hydroxyacylglutathione_hydrolase_MBL-fold | cd07723 | hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ... |
30-144 | 2.09e-10 | ||||||||
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Pssm-ID: 293809 [Multi-domain] Cd Length: 165 Bit Score: 59.40 E-value: 2.09e-10
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| Int9-11_CPSF2-3-like_MBL-fold | cd07734 | Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ... |
15-185 | 3.16e-10 | ||||||||
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain] Cd Length: 193 Bit Score: 59.65 E-value: 3.16e-10
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| ComEC | COG2333 | DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ... |
32-168 | 3.48e-10 | ||||||||
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: 60.64 E-value: 3.48e-10
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| RNaseZ_MBL-fold | cd16272 | Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ... |
13-168 | 4.47e-10 | ||||||||
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain] Cd Length: 180 Bit Score: 58.81 E-value: 4.47e-10
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| GloB | COG0491 | Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ... |
17-168 | 9.29e-10 | ||||||||
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only]; Pssm-ID: 440257 [Multi-domain] Cd Length: 215 Bit Score: 58.93 E-value: 9.29e-10
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| PDE1 | COG5212 | cAMP phosphodiesterase [Signal transduction mechanisms]; |
12-168 | 1.33e-09 | ||||||||
cAMP phosphodiesterase [Signal transduction mechanisms]; Pssm-ID: 444071 [Multi-domain] Cd Length: 300 Bit Score: 59.59 E-value: 1.33e-09
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| CcrA-like_MBL-B1 | cd16302 | Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ... |
32-117 | 2.86e-09 | ||||||||
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Pssm-ID: 293860 Cd Length: 212 Bit Score: 57.25 E-value: 2.86e-09
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| Lactamase_B | pfam00753 | Metallo-beta-lactamase superfamily; |
19-169 | 3.82e-09 | ||||||||
Metallo-beta-lactamase superfamily; Pssm-ID: 425851 [Multi-domain] Cd Length: 196 Bit Score: 56.61 E-value: 3.82e-09
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| metallo-hydrolase-like_MBL-fold | cd07743 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
32-109 | 2.48e-08 | ||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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) 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: 293829 [Multi-domain] Cd Length: 197 Bit Score: 54.07 E-value: 2.48e-08
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| flavodiiron_proteins_MBL-fold | cd07709 | catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ... |
66-169 | 6.79e-08 | ||||||||
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain. Pssm-ID: 293795 [Multi-domain] Cd Length: 238 Bit Score: 53.65 E-value: 6.79e-08
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| ComA-like_MBL-fold | cd07731 | Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ... |
21-143 | 9.31e-08 | ||||||||
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: 52.14 E-value: 9.31e-08
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| yflN-like_MBL-fold | cd07721 | uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ... |
21-109 | 1.01e-07 | ||||||||
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: 52.61 E-value: 1.01e-07
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| NorV | COG0426 | Flavorubredoxin [Energy production and conversion]; |
67-142 | 1.11e-07 | ||||||||
Flavorubredoxin [Energy production and conversion]; Pssm-ID: 440195 [Multi-domain] Cd Length: 390 Bit Score: 54.07 E-value: 1.11e-07
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| BaeB-like_MBL-fold | cd16275 | Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ... |
63-135 | 1.56e-07 | ||||||||
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain] Cd Length: 174 Bit Score: 51.38 E-value: 1.56e-07
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| PRK11921 | PRK11921 | anaerobic nitric oxide reductase flavorubredoxin; |
62-142 | 1.96e-07 | ||||||||
anaerobic nitric oxide reductase flavorubredoxin; Pssm-ID: 237023 [Multi-domain] Cd Length: 394 Bit Score: 53.54 E-value: 1.96e-07
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| COG1237 | COG1237 | Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only]; |
67-99 | 2.66e-07 | ||||||||
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only]; Pssm-ID: 440850 Cd Length: 273 Bit Score: 52.19 E-value: 2.66e-07
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| DHPS-like_MBL-fold | cd07713 | Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ... |
67-102 | 5.13e-07 | ||||||||
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: 51.47 E-value: 5.13e-07
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| class_II_PDE_MBL-fold | cd07735 | class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ... |
12-195 | 7.07e-07 | ||||||||
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821 Cd Length: 259 Bit Score: 50.67 E-value: 7.07e-07
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| INTS11-like_MBL-fold | cd16291 | Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ... |
13-116 | 9.37e-07 | ||||||||
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293849 Cd Length: 199 Bit Score: 49.57 E-value: 9.37e-07
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| YycJ-like_MBL-fold | cd07733 | uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ... |
66-184 | 4.10e-06 | ||||||||
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain] Cd Length: 151 Bit Score: 46.87 E-value: 4.10e-06
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| TTHA1623-like_MBL-fold | cd16322 | uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ... |
11-110 | 6.66e-06 | ||||||||
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode. Pssm-ID: 293877 [Multi-domain] Cd Length: 204 Bit Score: 47.34 E-value: 6.66e-06
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| RNaseZ_ZiPD-like_MBL-fold | cd07717 | Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ... |
13-149 | 1.13e-05 | ||||||||
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain] Cd Length: 247 Bit Score: 47.06 E-value: 1.13e-05
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| SNM1A-like_MBL-fold | cd16298 | 5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes ... |
70-172 | 1.17e-05 | ||||||||
5'-exonucleases human SNM1A and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) which is a 5'-exonuclease and functions in interstrand cross-links (ICL) repair. 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: 293856 [Multi-domain] Cd Length: 157 Bit Score: 45.58 E-value: 1.17e-05
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| LACTB2-like_MBL-fold | cd07722 | uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ... |
38-133 | 1.99e-05 | ||||||||
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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: 293808 [Multi-domain] Cd Length: 188 Bit Score: 45.60 E-value: 1.99e-05
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| ST1585-like_MBL-fold | cd07726 | uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ... |
13-99 | 2.01e-05 | ||||||||
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 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: 293812 [Multi-domain] Cd Length: 215 Bit Score: 45.95 E-value: 2.01e-05
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| RMMBL | pfam07521 | Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ... |
369-410 | 2.35e-05 | ||||||||
Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold contains five sequence motifs. The first four motifs are found in pfam00753 and are common to all metallo-beta-lactamases. This, the fifth motif, appears to be specific to Zn-dependent metallohydrolases such as ribonuclease J 2 which are involved in the processing of mRNA. This domain adds essential structural elements to the CASP-domain and is unique to RNA/DNA-processing nucleases, showing that they are pre-mRNA 3'-end-processing endonucleases. Pssm-ID: 462191 [Multi-domain] Cd Length: 63 Bit Score: 42.22 E-value: 2.35e-05
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| metallo-hydrolase-like_MBL-fold | cd07740 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
20-100 | 3.44e-05 | ||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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) 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: 293826 [Multi-domain] Cd Length: 194 Bit Score: 44.94 E-value: 3.44e-05
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| POD-like_MBL-fold | cd07724 | ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ... |
30-135 | 3.61e-05 | ||||||||
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes 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: 293810 [Multi-domain] Cd Length: 177 Bit Score: 44.70 E-value: 3.61e-05
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| Lactamase_B_2 | pfam12706 | Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
69-202 | 4.41e-05 | ||||||||
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753. Pssm-ID: 432732 [Multi-domain] Cd Length: 196 Bit Score: 44.61 E-value: 4.41e-05
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| PRK05452 | PRK05452 | anaerobic nitric oxide reductase flavorubredoxin; Provisional |
64-142 | 4.97e-05 | ||||||||
anaerobic nitric oxide reductase flavorubredoxin; Provisional Pssm-ID: 235475 [Multi-domain] Cd Length: 479 Bit Score: 45.90 E-value: 4.97e-05
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| PRK10241 | PRK10241 | hydroxyacylglutathione hydrolase; Provisional |
64-137 | 8.36e-05 | ||||||||
hydroxyacylglutathione hydrolase; Provisional Pssm-ID: 182327 [Multi-domain] Cd Length: 251 Bit Score: 44.43 E-value: 8.36e-05
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| metallo-hydrolase-like_MBL-fold | cd16279 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ... |
30-200 | 1.37e-04 | ||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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, 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. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B). Pssm-ID: 293837 [Multi-domain] Cd Length: 193 Bit Score: 43.23 E-value: 1.37e-04
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| arylsulfatase_AtsA-like_MBL-fold | cd07719 | Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ... |
21-168 | 1.38e-04 | ||||||||
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Pssm-ID: 293805 [Multi-domain] Cd Length: 193 Bit Score: 42.89 E-value: 1.38e-04
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| YcbL-like_MBL-fold | cd07737 | Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ... |
40-101 | 2.48e-04 | ||||||||
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain] Cd Length: 190 Bit Score: 42.15 E-value: 2.48e-04
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| UlaG | COG2220 | L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
62-199 | 2.75e-04 | ||||||||
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 441822 [Multi-domain] Cd Length: 224 Bit Score: 42.60 E-value: 2.75e-04
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| BcII-like_MBL-B1 | cd16304 | Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ... |
32-110 | 3.01e-04 | ||||||||
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Pssm-ID: 293862 [Multi-domain] Cd Length: 212 Bit Score: 42.27 E-value: 3.01e-04
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| PRK00055 | PRK00055 | ribonuclease Z; Reviewed |
17-113 | 3.11e-04 | ||||||||
ribonuclease Z; Reviewed Pssm-ID: 234602 [Multi-domain] Cd Length: 270 Bit Score: 42.86 E-value: 3.11e-04
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| metallo-hydrolase-like_MBL-fold | cd16280 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
22-134 | 1.05e-03 | ||||||||
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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, 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: 293838 [Multi-domain] Cd Length: 251 Bit Score: 41.03 E-value: 1.05e-03
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| IMP_DIM-like_MBL-B1 | cd16301 | IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ... |
59-119 | 1.08e-03 | ||||||||
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Pssm-ID: 293859 [Multi-domain] Cd Length: 215 Bit Score: 40.73 E-value: 1.08e-03
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| MBL-B1 | cd16285 | metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ... |
32-119 | 1.12e-03 | ||||||||
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. Pssm-ID: 293843 [Multi-domain] Cd Length: 210 Bit Score: 40.73 E-value: 1.12e-03
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| ComEC_Rec2 | TIGR00361 | DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ... |
21-94 | 2.03e-03 | ||||||||
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: 41.04 E-value: 2.03e-03
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| IND_BlaB-like_MBL-B1 | cd16299 | IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ... |
29-147 | 6.16e-03 | ||||||||
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Pssm-ID: 293857 Cd Length: 212 Bit Score: 38.19 E-value: 6.16e-03
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| PRK11539 | PRK11539 | ComEC family competence protein; Provisional |
21-101 | 9.09e-03 | ||||||||
ComEC family competence protein; Provisional Pssm-ID: 236924 [Multi-domain] Cd Length: 755 Bit Score: 38.82 E-value: 9.09e-03
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