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Conserved domains on  [gi|1265601662|gb|PGV13707|]
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cytoplasmic protein [Bacillus cereus]

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 6.01e-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: 6.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  13 KLTVFSSDEK-SFMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAVYPEAIA 91
Cdd:cd07739     2 QVDVFTAPEIsSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPDAKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  92 YATESTVEHIVHSVLGKLKVWKDALGENAPSNVVLPQVFKEKAIDFQGLTFELVGLDH----YRTSLFNKELKVLIGGID 167
Cdd:cd07739    82 VATPAVVAHIKAQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLEGHPLEIVGVGGgdtdDTTYLWIPSLKTVVAGDV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1265601662 168 VFNEIHVFLADTNSKAAMEAWIENLKVLQALHADIIVPSH 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 6.01e-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: 6.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  13 KLTVFSSDEK-SFMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAVYPEAIA 91
Cdd:cd07739     2 QVDVFTAPEIsSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPDAKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  92 YATESTVEHIVHSVLGKLKVWKDALGENAPSNVVLPQVFKEKAIDFQGLTFELVGLDH----YRTSLFNKELKVLIGGID 167
Cdd:cd07739    82 VATPAVVAHIKAQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLEGHPLEIVGVGGgdtdDTTYLWIPSLKTVVAGDV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1265601662 168 VFNEIHVFLADTNSKAAMEAWIENLKVLQALHADIIVPSH 207
Cdd:cd07739   162 VYNGVHVWLADATTPELRAAWLAALDKIEALNPETVVPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 24-208 7.63e-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: 71.65  E-value: 7.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  24 FMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAVYpEAIAYATESTVEHIVH 103
Cdd:COG0491    13 LGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662 104 svlgklkvwKDALGENAPSNVVLPQVFKEK-AIDFQGLTFELVGL-----DHyrTSLFNKELKVLIGGiD-VFNEIHVFL 176
Cdd:COG0491    92 ---------PAAGALFGREPVPPDRTLEDGdTLELGGPGLEVIHTpghtpGH--VSFYVPDEKVLFTG-DaLFSGGVGRP 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1265601662 177 ADTNskAAMEAWIENLKVLQALHADIIVPSHG 208
Cdd:COG0491   160 DLPD--GDLAQWLASLERLLALPPDLVIPGHG 189
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-207 2.27e-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: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662   27 TATLVEKAGHAFLINSKFtqSDSKEIVEYLKKNNLS-LDKIFIIHGDPDYYFGLESIKAVYPEAIaYATESTVEHIVHSV 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP--GEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPV-YAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  106 LGKLkvwkdALGENAPSNVVLPQVFKEKAIDFQGLTFELVGL-----DHyrTSLFNKELKVLIGGIDVFNEIHVFLADTN 180
Cdd:smart00849  78 ALLG-----ELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTpghtpGS--IVLYLPEGKILFTGDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 1265601662  181 SKAAMEAWIENLKVLQALHADIIVPSH 207
Cdd:smart00849 151 GDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
24-207 2.65e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 49.67  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  24 FMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKK-NNLSLDKIFIIHGDPDYYFGLESIKAVYPEAIAYATESTVEHIV 102
Cdd:pfam00753   4 GQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGlGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662 103 HSVLGKLKVWKDALGENAPSNVVLPQVFKEKAIDFQGLTFELVGLDHYRT--SLFNKELKVLIGGiD-VFNEIHVFLADT 179
Cdd:pfam00753  84 EELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGhvVVYYGGGKVLFTG-DlLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1265601662 180 NSKAAM------EAWIENLKVLQALHADIIVPSH 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 6.01e-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: 6.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  13 KLTVFSSDEK-SFMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAVYPEAIA 91
Cdd:cd07739     2 QVDVFTAPEIsSFPVTSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPDAKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  92 YATESTVEHIVHSVLGKLKVWKDALGENAPSNVVLPQVFKEKAIDFQGLTFELVGLDH----YRTSLFNKELKVLIGGID 167
Cdd:cd07739    82 VATPAVVAHIKAQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLEGHPLEIVGVGGgdtdDTTYLWIPSLKTVVAGDV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1265601662 168 VFNEIHVFLADTNSKAAMEAWIENLKVLQALHADIIVPSH 207
Cdd:cd07739   162 VYNGVHVWLADATTPELRAAWLAALDKIEALNPETVVPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 24-208 7.63e-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: 71.65  E-value: 7.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  24 FMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAVYpEAIAYATESTVEHIVH 103
Cdd:COG0491    13 LGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662 104 svlgklkvwKDALGENAPSNVVLPQVFKEK-AIDFQGLTFELVGL-----DHyrTSLFNKELKVLIGGiD-VFNEIHVFL 176
Cdd:COG0491    92 ---------PAAGALFGREPVPPDRTLEDGdTLELGGPGLEVIHTpghtpGH--VSFYVPDEKVLFTG-DaLFSGGVGRP 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1265601662 177 ADTNskAAMEAWIENLKVLQALHADIIVPSHG 208
Cdd:COG0491   160 DLPD--GDLAQWLASLERLLALPPDLVIPGHG 189
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-210 2.42e-14

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: 69.90  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  16 VFSSDEKSFMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKK-NNLSLDKIFIIHGDPDYYFGLesikAVYPEAIA--Y 92
Cdd:cd16282     5 LIGPDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKvTDKPVRYVVNTHYHGDHTLGN----AAFADAGApiI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  93 ATESTVEHIVHSVLGKLKVWKDALGENAP-SNVVLP-QVFKEKA-IDFQGLTFEL--VGLDHYRTSL--FNKELKVLIGG 165
Cdd:cd16282    81 AHENTREELAARGEAYLELMRRLGGDAMAgTELVLPdRTFDDGLtLDLGGRTVELihLGPAHTPGDLvvWLPEEGVLFAG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1265601662 166 iD-VFNEIHVFLADTNSKAameaWIENLKVLQALHADIIVPSHGSI 210
Cdd:cd16282   161 -DlVFNGRIPFLPDGSLAG----WIAALDRLLALDATVVVPGHGPV 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-207 2.27e-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: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662   27 TATLVEKAGHAFLINSKFtqSDSKEIVEYLKKNNLS-LDKIFIIHGDPDYYFGLESIKAVYPEAIaYATESTVEHIVHSV 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP--GEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPV-YAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  106 LGKLkvwkdALGENAPSNVVLPQVFKEKAIDFQGLTFELVGL-----DHyrTSLFNKELKVLIGGIDVFNEIHVFLADTN 180
Cdd:smart00849  78 ALLG-----ELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTpghtpGS--IVLYLPEGKILFTGDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 1265601662  181 SKAAMEAWIENLKVLQALHADIIVPSH 207
Cdd:smart00849 151 GDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
24-207 2.65e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 49.67  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  24 FMVTATLVEKAGHAFLINSKFTQSDSKEIVEYLKK-NNLSLDKIFIIHGDPDYYFGLESIKAVYPEAIAYATESTVEHIV 102
Cdd:pfam00753   4 GQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGlGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662 103 HSVLGKLKVWKDALGENAPSNVVLPQVFKEKAIDFQGLTFELVGLDHYRT--SLFNKELKVLIGGiD-VFNEIHVFLADT 179
Cdd:pfam00753  84 EELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGhvVVYYGGGKVLFTG-DlLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1265601662 180 NSKAAM------EAWIENLKVLQALHADIIVPSH 207
Cdd:pfam00753 163 LGGLLVlhpssaESSLESLLKLAKLKAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 24-208 6.28e-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: 42.98  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  24 FMVTATLVEKAGHAFLINSKFTQSdSKEIVEYLKKNNLS---LDKIFIIHGDPDYYFGLESIKAvYPEAIAYATESTVEH 100
Cdd:cd07721     9 PPVNAYLIEDDDGLTLIDTGLPGS-AKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKE-APGAPVYAHEREAPY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662 101 IvhsvLGKLKV-WKDALGENAPSNVVLPQVFKEKAIDFQ-GLTFELVG-----------LDHyrTSLFNKELKVLIGGiD 167
Cdd:cd07721    87 L----EGEKPYpPPVRLGLLGLLSPLLPVKPVPVDRTLEdGDTLDLAGglrvihtpghtPGH--ISLYLEEDGVLIAG-D 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1265601662 168 VFNEIHVFLADTNSKAA--MEAWIENLKVLQALHADIIVPSHG 208
Cdd:cd07721   160 ALVTVGGELVPPPPPFTwdMEEALESLRKLAELDPEVLAPGHG 202
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 47-111 2.21e-04

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: 40.91  E-value: 2.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265601662  47 SDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAVYPEAIAYA-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 ...
 28-143 8.63e-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: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  28 ATLVEKAGHAFLI----NSKFTQSDskeIVEYLK-KNNLSLDKIFIIHGDPDYYFGLESIKAVYPeaiayatestVEHIV 102
Cdd:cd07731    12 AILIQTPGKTILIdtgpRDSFGEDV---VVPYLKaRGIKKLDYLILTHPDADHIGGLDAVLKNFP----------VKEVY 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1265601662 103 HS-VLGKLKVWKDALGENAPSNVVLPQVFKEKAIDFQGLTFE 143
Cdd:cd07731    79 MPgVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFE 120
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-207 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) 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: 37.90  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  31 VEKAGHAFLINSKFTQSDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAvYPEAIAYATE---STVEHIV--HSV 105
Cdd:cd07743    14 VFGDKEALLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVYAPKiekAFIENPLlePSY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662 106 LGK---LKVWKDALGENAPSNVvlPQVFKEKAIDFQGLTFELVGLD-HYRTSL-FNKELKVL-----IGGIDVFNEIHV- 174
Cdd:cd07743    93 LGGaypPKELRNKFLMAKPSKV--DDIIEEGELELGGVGLEIIPLPgHSFGQIgILTPDGVLfagdaLFGEEVLEKYGIp 170

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1265601662 175 FLADtnskaaMEAWIENLKVLQALHADIIVPSH 207
Cdd:cd07743   171 FLYD------VEEQLETLEKLEELDADYYVPGH 197
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 30-207 3.28e-03

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: 37.65  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662  30 LVEKAGHAFLINSKFtqSDSKEIVEYLKKNNLSLDKIFIIHGDPDYYFGLESIKAvYPEAIAYATESTVEHIVHSVLGKL 109
Cdd:cd06262    15 VSDEEGEAILIDPGA--GALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKE-APGAPVYIHEADAELLEDPELNLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265601662 110 KVWKDALgeNAPSNVVLpqvFKEKA-IDFQGLTFELV---GldHYR--TSLFNKELKVLIGGiDV-FNEIHVF--LADTN 180
Cdd:cd06262    92 FFGGGPL--PPPEPDIL---LEDGDtIELGGLELEVIhtpG--HTPgsVCFYIEEEGVLFTG-DTlFAGSIGRtdLPGGD 163

                         170       180
                  ....*....|....*....|....*..
gi 1265601662 181 SKAAMEAWIENLKVLQAlhADIIVPSH 207
Cdd:cd06262   164 PEQLIESIKKLLLLLPD--DTVVYPGH 188
 
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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