MULTISPECIES: beta-CASP ribonuclease aCPSF1 [Picrophilus]
Protein Classification
beta-CASP ribonuclease aCPSF1( domain architecture ID 11497323)
archaeal beta-CASP ribonuclease 1 (aCPSF1) is an archaeal cleavage and polyadenylation specificity factor (CPSF) similar to methanothermobacter thermautotrophicus MTH1203, a metal-dependent ribonuclease
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| arCOG00543 | TIGR03675 | arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins ... |
7-638 | 0e+00 | |||||||||
arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins is universal in the archaea and consistsof an N-terminal type-1 KH-domain (pfam00013) a central beta-lactamase-domain (pfam00753) with a C-terminal motif associated with RNA metabolism (pfam07521). KH-domains are associated with RNA-binding, so taken together, this protein is a likely metal-dependent RNAase. This family was defined as arCOG01782. : Pssm-ID: 274718 [Multi-domain] Cd Length: 630 Bit Score: 1074.57 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| arCOG00543 | TIGR03675 | arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins ... |
7-638 | 0e+00 | |||||||||
arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins is universal in the archaea and consistsof an N-terminal type-1 KH-domain (pfam00013) a central beta-lactamase-domain (pfam00753) with a C-terminal motif associated with RNA metabolism (pfam07521). KH-domains are associated with RNA-binding, so taken together, this protein is a likely metal-dependent RNAase. This family was defined as arCOG01782. Pssm-ID: 274718 [Multi-domain] Cd Length: 630 Bit Score: 1074.57 E-value: 0e+00
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| COG1782 | COG1782 | Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ... |
179-637 | 0e+00 | |||||||||
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only]; Pssm-ID: 441388 [Multi-domain] Cd Length: 460 Bit Score: 674.92 E-value: 0e+00
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| TTHA0252-CPSF-like_MBL-fold | cd16295 | Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ... |
181-380 | 2.82e-76 | |||||||||
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: 241.59 E-value: 2.82e-76
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| Beta-Casp | smart01027 | Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ... |
423-548 | 7.47e-41 | |||||||||
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains. Pssm-ID: 214983 [Multi-domain] Cd Length: 126 Bit Score: 144.60 E-value: 7.47e-41
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| Beta-Casp | pfam10996 | Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ... |
424-546 | 1.66e-30 | |||||||||
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains. Pssm-ID: 463203 Cd Length: 109 Bit Score: 115.30 E-value: 1.66e-30
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| PRK02113 | PRK02113 | MBL fold metallo-hydrolase; |
192-251 | 3.71e-05 | |||||||||
MBL fold metallo-hydrolase; Pssm-ID: 179371 [Multi-domain] Cd Length: 252 Bit Score: 45.54 E-value: 3.71e-05
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| Name | Accession | Description | Interval | E-value | |||||||||
| arCOG00543 | TIGR03675 | arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins ... |
7-638 | 0e+00 | |||||||||
arCOG00543 universal archaeal KH-domain/beta-lactamase-domain protein; This family of proteins is universal in the archaea and consistsof an N-terminal type-1 KH-domain (pfam00013) a central beta-lactamase-domain (pfam00753) with a C-terminal motif associated with RNA metabolism (pfam07521). KH-domains are associated with RNA-binding, so taken together, this protein is a likely metal-dependent RNAase. This family was defined as arCOG01782. Pssm-ID: 274718 [Multi-domain] Cd Length: 630 Bit Score: 1074.57 E-value: 0e+00
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| COG1782 | COG1782 | Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ... |
179-637 | 0e+00 | |||||||||
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only]; Pssm-ID: 441388 [Multi-domain] Cd Length: 460 Bit Score: 674.92 E-value: 0e+00
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| YSH1 | COG1236 | RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ... |
180-607 | 1.75e-127 | |||||||||
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440849 [Multi-domain] Cd Length: 404 Bit Score: 381.84 E-value: 1.75e-127
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| TTHA0252-CPSF-like_MBL-fold | cd16295 | Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ... |
181-380 | 2.82e-76 | |||||||||
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: 241.59 E-value: 2.82e-76
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| Int9-11_CPSF2-3-like_MBL-fold | cd07734 | Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ... |
182-380 | 1.12e-44 | |||||||||
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: 157.88 E-value: 1.12e-44
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| Beta-Casp | smart01027 | Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ... |
423-548 | 7.47e-41 | |||||||||
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains. Pssm-ID: 214983 [Multi-domain] Cd Length: 126 Bit Score: 144.60 E-value: 7.47e-41
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| INTS11-like_MBL-fold | cd16291 | Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ... |
181-354 | 3.13e-31 | |||||||||
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: 120.44 E-value: 3.13e-31
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| Beta-Casp | pfam10996 | Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in ... |
424-546 | 1.66e-30 | |||||||||
Beta-Casp domain; The beta-CASP domain is found C terminal to the beta-lactamase domain in pre-mRNA 3'-end-processing endonuclease. The active site of this enzyme is located at the interface of these two domains. Pssm-ID: 463203 Cd Length: 109 Bit Score: 115.30 E-value: 1.66e-30
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| KH_7 | pfam17214 | KH domain; |
5-70 | 2.71e-26 | |||||||||
KH domain; Pssm-ID: 435791 Cd Length: 68 Bit Score: 101.86 E-value: 2.71e-26
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| CPSF3-like_MBL-fold | cd16292 | cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ... |
179-336 | 3.75e-26 | |||||||||
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: 106.13 E-value: 3.75e-26
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| KH-II_CPSF_arch_rpt2 | cd02410 | second type II K-homology (KH) RNA-binding domain found in archaeal cleavage and ... |
76-147 | 1.13e-20 | |||||||||
second type II K-homology (KH) RNA-binding domain found in archaeal cleavage and polyadenylation specificity factor (CPSF) and similar proteins; The archaeal CPSFs are predicted to be metal-dependent RNases belonging to the beta-CASP family, a subgroup of enzymes within the metallo-beta-lactamase fold. Within the CPSF family, all archaeal genomes contain one member with two N-terminal type II K-homology (KH) domains and one without. This family includes the CPSF homologs from archaea possessing N-terminal KH domains. This model corresponds to the second KH domain of CPSF, which is a canonical type II KH domain that contains the signature motif GXXG (where X represents any amino acid). Pssm-ID: 411781 Cd Length: 76 Bit Score: 86.15 E-value: 1.13e-20
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| Lactamase_B | smart00849 | Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ... |
193-358 | 1.07e-17 | |||||||||
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: 81.06 E-value: 1.07e-17
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| KH-II_CPSF_arch_rpt1 | cd22532 | first type II K-homology (KH) RNA-binding domain found in archaeal cleavage and ... |
6-66 | 7.44e-17 | |||||||||
first type II K-homology (KH) RNA-binding domain found in archaeal cleavage and polyadenylation specificity factor (CPSF) and similar proteins; The archaeal CPSFs are predicted to be metal-dependent RNases belonging to the beta-CASP family, a subgroup of enzymes within the metallo-beta-lactamase fold. Within the CPSF family, all archaeal genomes contain one member with two N-terminal type II K-homology (KH) domains and one without. This family includes the CPSF homologs from archaea possessing N-terminal KH domains. This model corresponds to the first KH domain, which is a non-canonical type II KH domain that does not contain the signature motif GXXG (where X represents any amino acid). Pssm-ID: 411789 Cd Length: 62 Bit Score: 74.94 E-value: 7.44e-17
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| CPSF2-like_MBL-fold | cd16293 | cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ... |
182-336 | 3.11e-16 | |||||||||
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component 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. This subgroup includes Ydh1p, the yeast homolog of CPSF2. 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. 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: 293851 Cd Length: 199 Bit Score: 77.56 E-value: 3.11e-16
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| metallo-hydrolase-like_MBL-fold | cd07732 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
180-274 | 6.60e-15 | |||||||||
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: 73.80 E-value: 6.60e-15
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| RMMBL | pfam07521 | Zn-dependent metallo-hydrolase RNA specificity domain; The metallo-beta-lactamase fold ... |
565-627 | 1.14e-13 | |||||||||
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: 66.10 E-value: 1.14e-13
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| RnjA | COG0595 | mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; |
179-427 | 1.28e-12 | |||||||||
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440360 [Multi-domain] Cd Length: 553 Bit Score: 70.48 E-value: 1.28e-12
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| Lactamase_B_6 | pfam16661 | Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ... |
196-334 | 3.76e-11 | |||||||||
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase superfamily. Pssm-ID: 406948 Cd Length: 192 Bit Score: 62.61 E-value: 3.76e-11
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| Lactamase_B | pfam00753 | Metallo-beta-lactamase superfamily; |
188-354 | 1.07e-10 | |||||||||
Metallo-beta-lactamase superfamily; Pssm-ID: 425851 [Multi-domain] Cd Length: 196 Bit Score: 61.23 E-value: 1.07e-10
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| RNaseJ_MBL-fold | cd07714 | RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ... |
182-360 | 2.43e-10 | |||||||||
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: 61.27 E-value: 2.43e-10
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| RNaseZ_MBL-fold | cd16272 | Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ... |
193-354 | 2.12e-09 | |||||||||
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: 57.27 E-value: 2.12e-09
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| PhnP | COG1235 | Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ... |
173-280 | 6.92e-08 | |||||||||
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; Pssm-ID: 440848 [Multi-domain] Cd Length: 259 Bit Score: 54.13 E-value: 6.92e-08
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| ElaC | COG1234 | Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; |
179-283 | 8.08e-08 | |||||||||
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440847 [Multi-domain] Cd Length: 250 Bit Score: 53.66 E-value: 8.08e-08
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| AHL_lactonase_MBL-fold | cd07729 | quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ... |
196-354 | 4.14e-07 | |||||||||
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. 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: 293815 [Multi-domain] Cd Length: 238 Bit Score: 51.45 E-value: 4.14e-07
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| metallo-hydrolase-like_MBL-fold | cd16279 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ... |
192-273 | 4.21e-07 | |||||||||
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: 50.55 E-value: 4.21e-07
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| ComA-like_MBL-fold | cd07731 | Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ... |
194-285 | 8.65e-07 | |||||||||
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: 49.44 E-value: 8.65e-07
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| ComEC | COG2333 | DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ... |
180-285 | 2.29e-06 | |||||||||
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: 49.47 E-value: 2.29e-06
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| RNaseZ_short-form-like_MBL-fold | cd07716 | uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ... |
180-293 | 1.11e-05 | |||||||||
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: 46.28 E-value: 1.11e-05
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| LACTB2-like_MBL-fold | cd07722 | uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ... |
196-291 | 3.47e-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: 44.83 E-value: 3.47e-05
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| PRK02113 | PRK02113 | MBL fold metallo-hydrolase; |
192-251 | 3.71e-05 | |||||||||
MBL fold metallo-hydrolase; Pssm-ID: 179371 [Multi-domain] Cd Length: 252 Bit Score: 45.54 E-value: 3.71e-05
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| GloB | COG0491 | Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ... |
194-354 | 6.23e-05 | |||||||||
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: 44.68 E-value: 6.23e-05
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| yflN-like_MBL-fold | cd07721 | uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ... |
194-354 | 7.61e-05 | |||||||||
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: 44.13 E-value: 7.61e-05
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| MBLAC1-like_MBL-fold | cd07711 | uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ... |
195-291 | 8.50e-05 | |||||||||
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 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. Pssm-ID: 293797 [Multi-domain] Cd Length: 190 Bit Score: 43.73 E-value: 8.50e-05
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| Lactamase_B_2 | pfam12706 | Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
204-276 | 1.46e-04 | |||||||||
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: 43.07 E-value: 1.46e-04
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| UlaG | COG2220 | L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
177-331 | 3.20e-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: 3.20e-04
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| SNM1A-1C-like_MBL-fold | cd16273 | SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; ... |
242-344 | 3.51e-04 | |||||||||
SNM1A , artemis/SNM1C, yeast Pso2p, and related proteins; MBL-fold metallo-hydrolase domain; Includes human SNM1A (SNM1 homolog A, also known as DNA cross-link repair 1A protein) and Saccharomyces cerevisiae Pso2 protein (PSOralen derivative sensitive 2, also known as SNM1, sensitive to nitrogen mustard 1), both proteins are 5'-exonucleases and function in interstrand cross-links (ICL) repair. Also includes the nuclease artemis (also known as SNM1C, SNM1 homolog C, SNM1-like protein, and DNA cross-link repair 1C protein) which plays a role in V(D)J recombination/DNA repair. Purified artemis protein possesses single-strand-specific 5' to 3' exonuclease activity. Upon complex formation with, and phosphorylation by, DNA-dependent protein kinase, artemis gains endonucleolytic activity on hairpins and 5' and 3' overhangs. 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: 293831 Cd Length: 160 Bit Score: 41.37 E-value: 3.51e-04
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| metallo-hydrolase-like_MBL-fold | cd06262 | mainly hydrolytic enzymes and related proteins which carry out various biological functions; ... |
196-275 | 3.61e-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: 41.89 E-value: 3.61e-04
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| PDE1 | COG5212 | cAMP phosphodiesterase [Signal transduction mechanisms]; |
180-282 | 3.76e-04 | |||||||||
cAMP phosphodiesterase [Signal transduction mechanisms]; Pssm-ID: 444071 [Multi-domain] Cd Length: 300 Bit Score: 43.02 E-value: 3.76e-04
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| YycJ-like_MBL-fold | cd07733 | uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ... |
194-303 | 1.12e-03 | |||||||||
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: 39.94 E-value: 1.12e-03
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| BaeB-like_MBL-fold | cd16275 | Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ... |
237-354 | 1.41e-03 | |||||||||
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: 39.83 E-value: 1.41e-03
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| ST1585-like_MBL-fold | cd07726 | uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ... |
237-266 | 2.14e-03 | |||||||||
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: 39.78 E-value: 2.14e-03
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| metallo-hydrolase-like_MBL-fold | cd16281 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
196-251 | 2.48e-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: 293839 Cd Length: 252 Bit Score: 40.17 E-value: 2.48e-03
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| class_II_PDE_MBL-fold | cd07735 | class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ... |
180-253 | 2.66e-03 | |||||||||
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: 39.89 E-value: 2.66e-03
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| metallo-hydrolase-like_MBL-fold | cd07741 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
195-251 | 2.85e-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) 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: 293827 [Multi-domain] Cd Length: 212 Bit Score: 39.48 E-value: 2.85e-03
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| metallo-hydrolase-like_MBL-fold | cd07740 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
182-276 | 3.45e-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) 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: 39.16 E-value: 3.45e-03
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| ComEC_Rec2 | TIGR00361 | DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ... |
194-251 | 5.14e-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: 39.88 E-value: 5.14e-03
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| Int9-like_MBL-fold | cd16294 | integrator subunit 9, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a ... |
179-337 | 5.31e-03 | |||||||||
integrator subunit 9, 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 Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74). 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: 293852 [Multi-domain] Cd Length: 166 Bit Score: 38.25 E-value: 5.31e-03
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| MBL-B1 | cd16285 | metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ... |
196-276 | 6.79e-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: 38.42 E-value: 6.79e-03
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