![](files/infoQ.gif)
cytidine monophosphate-N-acetylneuraminic acid hydroxylase isoform X2 [Cricetulus griseus]
MBL fold metallo-hydrolase( domain architecture ID 11454817)
MBL fold metallo-hydrolase similar to as Sus scrofa cytidine monophosphate-N-acetylneuraminic acid hydroxylase and Bacillus subtilis UPF0173 protein YddR; may be inactive as a hydrolase such as human inactive cytidine monophosphate-N-acetylneuraminic CMAHP
List of domain hits
![](files/help.png)
Name | Accession | Description | Interval | E-value | |||
UlaG | COG2220 | L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
31-149 | 1.69e-15 | |||
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism]; : Pssm-ID: 441822 [Multi-domain] Cd Length: 224 Bit Score: 75.34 E-value: 1.69e-15
|
|||||||
Name | Accession | Description | Interval | E-value | |||
UlaG | COG2220 | L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
31-149 | 1.69e-15 | |||
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 441822 [Multi-domain] Cd Length: 224 Bit Score: 75.34 E-value: 1.69e-15
|
|||||||
Lactamase_B_3 | pfam13483 | Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
34-104 | 9.69e-07 | |||
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753. Pssm-ID: 433247 [Multi-domain] Cd Length: 160 Bit Score: 48.36 E-value: 9.69e-07
|
|||||||
PRK00685 | PRK00685 | metal-dependent hydrolase; Provisional |
33-97 | 2.08e-06 | |||
metal-dependent hydrolase; Provisional Pssm-ID: 234811 [Multi-domain] Cd Length: 228 Bit Score: 48.65 E-value: 2.08e-06
|
|||||||
RomA-like_MBL-fold | cd16283 | Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ... |
58-154 | 5.08e-06 | |||
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841 Cd Length: 181 Bit Score: 46.89 E-value: 5.08e-06
|
|||||||
Name | Accession | Description | Interval | E-value | |||
UlaG | COG2220 | L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ... |
31-149 | 1.69e-15 | |||
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 441822 [Multi-domain] Cd Length: 224 Bit Score: 75.34 E-value: 1.69e-15
|
|||||||
Lactamase_B_3 | pfam13483 | Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ... |
34-104 | 9.69e-07 | |||
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753. Pssm-ID: 433247 [Multi-domain] Cd Length: 160 Bit Score: 48.36 E-value: 9.69e-07
|
|||||||
PRK00685 | PRK00685 | metal-dependent hydrolase; Provisional |
33-97 | 2.08e-06 | |||
metal-dependent hydrolase; Provisional Pssm-ID: 234811 [Multi-domain] Cd Length: 228 Bit Score: 48.65 E-value: 2.08e-06
|
|||||||
RomA-like_MBL-fold | cd16283 | Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ... |
58-154 | 5.08e-06 | |||
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841 Cd Length: 181 Bit Score: 46.89 E-value: 5.08e-06
|
|||||||
metallo-hydrolase-like_MBL-fold | cd07732 | uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ... |
73-183 | 1.22e-03 | |||
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: 39.90 E-value: 1.22e-03
|
|||||||
ElaC | COG1234 | Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; |
45-115 | 6.75e-03 | |||
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440847 [Multi-domain] Cd Length: 250 Bit Score: 38.25 E-value: 6.75e-03
|
|||||||
Blast search parameters | ||||
|