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Conserved domains on  [gi|657627613|ref|WP_029438381|]
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MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-207 4.39e-55

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.


The actual alignment was detected with superfamily member cd07739:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 201  Bit Score: 176.15  E-value: 4.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  13 KLTVFSSDEK-SFMVTATLVEKAEHAFLINSKFTQSDSKEIIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYPEAIA 91
Cdd:cd07739    2 QVDVFTAPEIsSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPDAKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  92 YATESTVEHIVHSVLGKLKVWKDALGENAPSNVVLPQVFKEKSIDFQELTFELVGLD----DYRTSLFNRELKLLIGGID 167
Cdd:cd07739   82 VATPAVVAHIKAQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLEGHPLEIVGVGggdtDDTTYLWIPSLKTVVAGDV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 657627613 168 VFNEIHLFLADTSSKAAMEAWIENLRVLQALQADVIVPSH 207
Cdd:cd07739  162 VYNGVHVWLADATTPELRAAWLAALDKIEALNPETVVPGH 201
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-207 4.39e-55

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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 176.15  E-value: 4.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  13 KLTVFSSDEK-SFMVTATLVEKAEHAFLINSKFTQSDSKEIIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYPEAIA 91
Cdd:cd07739    2 QVDVFTAPEIsSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPDAKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  92 YATESTVEHIVHSVLGKLKVWKDALGENAPSNVVLPQVFKEKSIDFQELTFELVGLD----DYRTSLFNRELKLLIGGID 167
Cdd:cd07739   82 VATPAVVAHIKAQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLEGHPLEIVGVGggdtDDTTYLWIPSLKTVVAGDV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 657627613 168 VFNEIHLFLADTSSKAAMEAWIENLRVLQALQADVIVPSH 207
Cdd:cd07739  162 VYNGVHVWLADATTPELRAAWLAALDKIEALNPETVVPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 24-238 3.56e-15

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: 72.42  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  24 FMVTATLVEKAEHAFLINSKFTQSDSKEIIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYpEAIAYATESTVEHIVH 103
Cdd:COG0491   13 LGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613 104 svlgklkvwKDALGENAPSNVVLPQVFKEK-SIDFQELTFELVGLD---DYRTSLFNRELKLLIGGiD-VFNEIHLFLAD 178
Cdd:COG0491   92 ---------PAAGALFGREPVPPDRTLEDGdTLELGGPGLEVIHTPghtPGHVSFYVPDEKVLFTG-DaLFSGGVGRPDL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613 179 TSskAAMEAWIENLRVLQALQADVIVPSHGSIeksldnqAITATMDYLRTAIQASEESKN 238
Cdd:COG0491  162 PD--GDLAQWLASLERLLALPPDLVIPGHGPP-------TTAEAIDYLEELLAALGERAN 212
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-207 2.36e-11

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: 61.03  E-value: 2.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613    27 TATLVEKAEHAFLINSKFtqSDSKEIIDYLKKNNLS-LDKIFIIHGDPDYYFGLEGIKAAYPEAIaYATESTVEHIVHSV 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP--GEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPV-YAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613   106 LGKLkvwkdALGENAPSNVVLPQVFKEKSIDFQELTFELV---GLDDYRTSLFNRELKLLIGGIDVFNEIHLFLADTSSK 182
Cdd:smart00849  78 ALLG-----ELGAEAEPAPPDRTLKDGDELDLGGGELEVIhtpGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 657627613   183 AAMEAWIENLRVLQALQADVIVPSH 207
Cdd:smart00849 153 AAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
24-207 2.19e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 50.06  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613   24 FMVTATLVEKAEHAFLINSKFTQSDSKE-IIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYPEAIAYATESTVEHIv 102
Cdd:pfam00753   4 GQVNSYLIEGGGGAVLIDTGGSAEAALLlLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELL- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  103 HSVLGKLKVWKDALGENAPSNVVLPQVFKEKSIDFQELTFELV---GLDDYRTSLFNRELKLLIGG------IDVFNEIH 173
Cdd:pfam00753  83 DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVThgpGHGPGHVVVYYGGGKVLFTGdllfagEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 657627613  174 LFLADTSSKAAMEAWIENLRVLQALQADVIVPSH 207
Cdd:pfam00753 163 LGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-207 4.39e-55

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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 176.15  E-value: 4.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  13 KLTVFSSDEK-SFMVTATLVEKAEHAFLINSKFTQSDSKEIIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYPEAIA 91
Cdd:cd07739    2 QVDVFTAPEIsSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPDAKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  92 YATESTVEHIVHSVLGKLKVWKDALGENAPSNVVLPQVFKEKSIDFQELTFELVGLD----DYRTSLFNRELKLLIGGID 167
Cdd:cd07739   82 VATPAVVAHIKAQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLEGHPLEIVGVGggdtDDTTYLWIPSLKTVVAGDV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 657627613 168 VFNEIHLFLADTSSKAAMEAWIENLRVLQALQADVIVPSH 207
Cdd:cd07739  162 VYNGVHVWLADATTPELRAAWLAALDKIEALNPETVVPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 24-238 3.56e-15

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: 72.42  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  24 FMVTATLVEKAEHAFLINSKFTQSDSKEIIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYpEAIAYATESTVEHIVH 103
Cdd:COG0491   13 LGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613 104 svlgklkvwKDALGENAPSNVVLPQVFKEK-SIDFQELTFELVGLD---DYRTSLFNRELKLLIGGiD-VFNEIHLFLAD 178
Cdd:COG0491   92 ---------PAAGALFGREPVPPDRTLEDGdTLELGGPGLEVIHTPghtPGHVSFYVPDEKVLFTG-DaLFSGGVGRPDL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613 179 TSskAAMEAWIENLRVLQALQADVIVPSHGSIeksldnqAITATMDYLRTAIQASEESKN 238
Cdd:COG0491  162 PD--GDLAQWLASLERLLALPPDLVIPGHGPP-------TTAEAIDYLEELLAALGERAN 212
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-210 1.17e-13

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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 67.98  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  16 VFSSDEKSFMVTATLVEKAEHAFLINSKFTQSDSKEIIDYLKK-NNLSLDKIFIIHGDPDYYFGLegikAAYPEAIA--Y 92
Cdd:cd16282    5 LIGPDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKvTDKPVRYVVNTHYHGDHTLGN----AAFADAGApiI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  93 ATESTVEHIVHSVLGKLKVWKDALGENAP-SNVVLP-QVFKEK-SIDFQELTFELVGL------DDyrTSLFNRELKLLI 163
Cdd:cd16282   81 AHENTREELAARGEAYLELMRRLGGDAMAgTELVLPdRTFDDGlTLDLGGRTVELIHLgpahtpGD--LVVWLPEEGVLF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 657627613 164 GGiD-VFNEIHLFLADTSSKAameaWIENLRVLQALQADVIVPSHGSI 210
Cdd:cd16282  159 AG-DlVFNGRIPFLPDGSLAG----WIAALDRLLALDATVVVPGHGPV 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-207 2.36e-11

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: 61.03  E-value: 2.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613    27 TATLVEKAEHAFLINSKFtqSDSKEIIDYLKKNNLS-LDKIFIIHGDPDYYFGLEGIKAAYPEAIaYATESTVEHIVHSV 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP--GEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPV-YAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613   106 LGKLkvwkdALGENAPSNVVLPQVFKEKSIDFQELTFELV---GLDDYRTSLFNRELKLLIGGIDVFNEIHLFLADTSSK 182
Cdd:smart00849  78 ALLG-----ELGAEAEPAPPDRTLKDGDELDLGGGELEVIhtpGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 657627613   183 AAMEAWIENLRVLQALQADVIVPSH 207
Cdd:smart00849 153 AAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
24-207 2.19e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 50.06  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613   24 FMVTATLVEKAEHAFLINSKFTQSDSKE-IIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYPEAIAYATESTVEHIv 102
Cdd:pfam00753   4 GQVNSYLIEGGGGAVLIDTGGSAEAALLlLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELL- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  103 HSVLGKLKVWKDALGENAPSNVVLPQVFKEKSIDFQELTFELV---GLDDYRTSLFNRELKLLIGG------IDVFNEIH 173
Cdd:pfam00753  83 DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVThgpGHGPGHVVVYYGGGKVLFTGdllfagEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 657627613  174 LFLADTSSKAAMEAWIENLRVLQALQADVIVPSH 207
Cdd:pfam00753 163 LGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 24-208 1.02e-06

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: 47.99  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  24 FMVTATLVEKAEHAFLINSKFTQSdSKEIIDYLKKNNLS---LDKIFIIHGDPDYYFGLEGIKAAyPEAIAYATESTVEH 100
Cdd:cd07721    9 PPVNAYLIEDDDGLTLIDTGLPGS-AKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEA-PGAPVYAHEREAPY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613 101 IvhsvLGKLKVwkdalgENAPSNVVLPQVFKEKSIDFQELTFELVGLDDYR-----------------TSLFNRELKLLI 163
Cdd:cd07721   87 L----EGEKPY------PPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDlagglrvihtpghtpghISLYLEEDGVLI 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 657627613 164 GGiDVFNEIHLFLADTSSKAA--MEAWIENLRVLQALQADVIVPSHG 208
Cdd:cd07721  157 AG-DALVTVGGELVPPPPPFTwdMEEALESLRKLAELDPEVLAPGHG 202
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 47-111 8.04e-06

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: 45.14  E-value: 8.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657627613  47 SDSKEIIDYLKKNNLSLDKIFIIHGDPDYYFGLEGIKAAYPEAIAYA-TESTVEHIVHSV-------LGKLKV 111
Cdd:cd07723   28 GEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRIPGLDHPVkdgdeikLGGLEV 100
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 28-207 6.82e-04

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: 39.42  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613  28 ATLVEKAEHAFLI----NSKFTQSDskeIIDYLK-KNNLSLDKIFIIHGDPDYYFGLEGIKAAYPeaiayatestVEHIV 102
Cdd:cd07731   12 AILIQTPGKTILIdtgpRDSFGEDV---VVPYLKaRGIKKLDYLILTHPDADHIGGLDAVLKNFP----------VKEVY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657627613 103 HS-VLGKLKVWKDALGENAPSNVVLPQVFKEKSIDFQELTFELVG-LDDYRTSLFNRE--LKLLIGGIDVfneihLFLAD 178
Cdd:cd07731   79 MPgVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLSpPKDDYDDLNNNScvLRLTYGGTSF-----LLTGD 153

                        170       180       190
                 ....*....|....*....|....*....|
gi 657627613 179 TSSKAamEAWIenLRVLQALQADVI-VPSH 207
Cdd:cd07731  154 AEKEA--EEEL--LASGPDLLADVLkVGHH 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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